A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria (491 views)
Febs J (ISSN: 1742-464x), 2015 Apr 3; 282(13): 2500-2511.
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Paper type: Journal Article,
Impact factor: 4.237, 5-year impact factor: 4.082
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84929242634&partnerID=40&md5=032f49345d3ff252ca446b37f92a7bb0
Keywords: Dormant Mycobacteria, Muropeptides, Peptidoglycan, Rpfb, Bacterial Enzyme, Chemical Compound, N Acetylglucosaminyl B (1-4) N Acetylmuramyl Alanyl Dextro Isoglutamate, Resuscitation Promoting Factor Interacting Protein A, Resuscitation Promoting Factor Protein B, Unclassified Drug, Bacterial Protein, Cytokine, Resuscitation-Promoting Factor, Article, Concentration Response, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Dynamics, Molecular Weight, Mycobacterium Smegmatis, Nonhuman, Priority Journal, Protein Domain, Protein Function, Protein Hydrolysis, Digestion, Metabolism, Physiology, Actinobacteria, Corynebacterineae,
Affiliations:
*** IBB - CNR ***
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33 (2), 119071, Moscow.,
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russia
Institute of Biostructures and Bioimaging C.N.R. Napoli Italy
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33 (2), Moscow, Russian Federation
References:
Kaprelyants, A.S., Kell, D.B., Dormancy in stationary-phase cultures of Micrococcus luteus: Flow cytometric analysis of starvation and resuscitation (1993) Appl Environ Microbiol, 59, pp. 3187-319
Kana, B.D., Gordhan, B.G., Downing, K.J., Sung, N., Vostroktunova, G., Machowski, E.E., Tsenova, L., Kaplan, G., The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in vitro (2008) Mol Microbiol, 67, pp. 672-684
Kana, B.D., Mizrahi, V., Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling (2010) FEMS Immunol Med Microbiol, 58, pp. 39-50
Lillebaek, T., Dirksen, A., Baess, I., Strunge, B., Thomsen VØ., Andersen, A.B., Molecular evidence of endogenous reactivation of Mycobacterium tuberculosis after 33 years of latent infection (2002) J Infect Dis, 185, pp. 401-404
Wu, X., Yang, Y., Han, Y., Zhang, J., Liang, Y., Li, H., Li, B., Wang, L., Effect of recombinant Rv1009 protein on promoting the growth of Mycobacterium tuberculosis (2008) J Appl Microbiol, 105, pp. 1121-1127
Mukamolova, G.V., Turapov, O., Malkin, J., Woltmann, G., Barer, M.R., Resuscitation-promoting factors reveal an occult population of tubercle Bacilli in Sputum (2010) Am J Respir Crit Care Med, 181, pp. 174-180
Downing, K.J., Mischenko, V.V., Shleeva, M.O., Young, D.I., Young, M., Kaprelyants, A.S., Apt, A.S., Mizrahi, V., Mutants of Mycobacterium tuberculosis lacking three of the five rpf-like genes are defective for growth in vivo and for resuscitation in vitro (2005) Infect Immun, 73, pp. 3038-3043
Tufariello, J.M., Mi, K., Xu, J., Manabe, Y.C., Kesavan, A.K., Drumm, J., Tanaka, K., Chan, J., Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis (2006) Infect Immun, 74, pp. 2985-2995
Biketov, S., Potapov, V., Ganina, E., Downing, K., Kana, B.D., Kaprelyants, A., The role of resuscitation promoting factors in pathogenesis and reactivation of Mycobacterium tuberculosis during intra-peritoneal infection in mice (2007) BMC, 17, p. 146
Cohen-Gonsaud, M., Barthe, P., Bagnéris, C., Henderson, B., Ward, J., Roumestand, C., Keep, N.H., The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes (2005) Nat Struct Mol Biol, 12, pp. 270-273
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. Tuberculosis (2009) J Mol Biol, 385, pp. 153-162
Mukamolova, G.V., Murzin, A.G., Salina, E.G., Demina, G.R., Kell, D.B., Kaprelyants, A.S., Young, M., Muralytic activity of Micrococcus luteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation (2006) Mol Microbiol, 59, pp. 84-98
Telkov, M.V., Demina, G.R., Voloshin, S.A., Salina, E.G., Dudik, T.V., Stekhanova, T.N., Mukamolova, G.V., Young, M., Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycanhydrolases (2006) Biochemistry (Mosc), 71, pp. 414-422
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis (2013) J Biomol Struct Dyn, 31, pp. 195-205
Ruggiero, A., Squeglia, F., Esposito, C., Marasco, D., Pedone, E., Pedone, C., Berisio, R., Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M. Tuberculosis (2010) Protein Pept Lett, 17, pp. 70-73
Hett, E.C., Chao, M.C., Steyn, A.J., Fortune, S.M., Deng, L.L., Rubin, E.J., A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis (2007) Mol Microbiol, 66, pp. 658-668
Squeglia, F., Ruggiero, A., Romano, M., Vitagliano, L., Berisio, R., Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: Evidence for the L-to-D inversion of configuration of the catalytic cysteine (2014) Acta Crystallogr D Biol Crystallogr, 70, pp. 2295-2300
Brennan, P.J., Nikaido, H., The envelope of mycobacteria (1995) Annu Rev Biochem, 64, pp. 29-63
Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Mainardi, J.L., The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L D-transpeptidation (2008) J Bacteriol, 190, pp. 4360-4366
Vollmer, W., Höltje, J.V., The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)? (2004) J Bacteriol, 186, pp. 5978-5987
Brennan, P.J., Crick, D.C., The cell-wall core of Mycobacterium tuberculosis in the context of drug discovery (2007) Curr Top Med Chem, 7, pp. 475-488
Gupta, R., Lavollay, M., Mainardi, J.L., Arthur, M., Bishai, W.R., Lamichhane, G., The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin (2010) Nat Med, 16, pp. 466-469
Correale, S., Ruggiero, A., Capparelli, R., Pedone, E., Berisio, R., Structures of free and inhibited forms of the L, D-transpeptidase LdtMt1 from Mycobacterium tuberculosis (2013) Acta Crystallogr D Biol Crystallogr, 69, pp. 1697-1706
Priyadarshini, R., Popham, D.L., Young, K.D., Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli (2006) J Bacteriol, 188, pp. 5345-5355
Heidrich, C., Ursinus, A., Berger, J., Schwarz, H., Höltje, J.V., Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli (2002) J Bacteriol, 184, pp. 6093-6099
Nikitushkin, V.D., Demina, G.R., Shleeva, M.O., Kaprelyants, A.S., Peptidoglycan fragments stimulate resuscitation of "non-culturable" mycobacteria (2013) Antonie Van Leeuwenhoek, 103, pp. 37-46
Squeglia, F., Romano, M., Ruggiero, A., Vitagliano, L., De Simone, A., Berisio, R., Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses (2013) Biophys J, 104, pp. 2530-2539
Chao, M.C., Kieser, K.J., Minami, S., Mavrici, D., Aldridge, B.B., Fortune, S.M., Alber, T., Rubin, E.J., Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria (2013) PLoS Pathog, 9, p. e1003197
Shleeva, M., Mukamolova, G.V., Young, M., Williams, H.D., Kaprelyants, A.S., Formation of 'non-culturable' cells of Mycobacterium smegmatis in stationary phase in response to growth under suboptimal conditions and their Rpf-mediated resuscitation (2004) Microbiology, 150, pp. 1687-1697
Matsushima, Y., Miyazaki, T., Kasai, S., Chemical evidence for the Phillips model of the action of hen egg white lysozyme (1968) Nature, 219, p. 265
Vocadlo, D.J., Davies, G.J., Laine, R., Withers, S.G., Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate (2001) Nature, 412, pp. 835-838
Phillips, D.C., The hen egg white lysozyme molecule (1967) Proc Natl Acad Sci USA, 57, pp. 483-495
Höltje, J.V., Mirelman, D., Sharon, N., Schwarz, U., Novel type of murein transglycosylase in Escherichia coli (1975) J Bacteriol, 124, pp. 1067-1076
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135, pp. 486-496
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J Am Chem Soc, 133, pp. 20676-20679
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr Protein Pept Sci, 13, pp. 756-766
Lee, M., Hesek, D., Shah, I.M., Oliver, A.G., Dworkin, J., Mobashery, S., Synthetic peptidoglycan motifs for germination of bacterial spores (2010) ChemBioChem, 11, pp. 2525-2529
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G.J., Husson, R.N., The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization (2011) PLoS Pathog, 7, p. e1002182
Park, J.T., Uehara, T., How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan) (2008) Microbiol Mol Biol Rev, 72, pp. 211-227
Reith, J., Mayer, C., Peptidoglycanturnover and recycling in Gram-positive bacteria (2011) Appl Microbiol Biotechnol, 92, pp. 1-11
Höltje, J.V., Kopp, U., Ursinus, A., Wiedemann, B., The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase (1994) FEMS Microbiol Lett, 122, pp. 159-164
Prigozhin, D.M., Mavrici, D., Huizar, J.P., Vansell, H.J., Alber, T., Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-L-alanine amidase Rv3717 point to a role in peptidoglycanfragment recycling (2013) J Biol Chem, 288, pp. 31549-31555
Parish, T., Stocker, N., Methods in molecular Biology (1998) Mycobacteria Protocols, pp. 91-107. , Humana Press, Totowa, NJ
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (2010) Structure, 18, pp. 1184-1190
Rostovtseva, L., Andronova, T., Malkova, V., Sorokina, I., Ivaniv, V., Synthesis and antitumor activity of glycopeptides containing N-Acetylglucosaminil-(ß 1-4)-N-acetylmuramyl disaccharide unit (1981) Bioorg Khim, 12, pp. 1843-1858. , Russian
Hoshino, O., Zehavi, U., Sîna, P., Jeanloz, R.W., The isolation and structure identification of a discaccharide containing manno-muramic acid from Micrococcus lysodeikticus cell wall (1972) J Biol Chem, 247, pp. 381-390
Zemlyakov, A., Synthesis of γ-benzyl tert-butoxycarbonyl-L-alanyl-D-glutamate and its derivatives (1998) Chem Nat Compd, 34, pp. 78-79
Chun, Y., Yan, S., Li, X., Ding, N., Zhang, W., Wang, P., Li, M., Li, Y., Synthesis of 1,6-anhydro sugars catalyzed by silica supported perchloric acid (2011) Tetrahedron Lett, 52, pp. 6196-6198
Febs J (ISSN: 1742-464x), 2015 Apr 3; 282(13): 2500-2511.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.237, 5-year impact factor: 4.082
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84929242634&partnerID=40&md5=032f49345d3ff252ca446b37f92a7bb0
Keywords: Dormant Mycobacteria, Muropeptides, Peptidoglycan, Rpfb, Bacterial Enzyme, Chemical Compound, N Acetylglucosaminyl B (1-4) N Acetylmuramyl Alanyl Dextro Isoglutamate, Resuscitation Promoting Factor Interacting Protein A, Resuscitation Promoting Factor Protein B, Unclassified Drug, Bacterial Protein, Cytokine, Resuscitation-Promoting Factor, Article, Concentration Response, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Dynamics, Molecular Weight, Mycobacterium Smegmatis, Nonhuman, Priority Journal, Protein Domain, Protein Function, Protein Hydrolysis, Digestion, Metabolism, Physiology, Actinobacteria, Corynebacterineae,
Affiliations:
*** IBB - CNR ***
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33 (2), 119071, Moscow.,
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russia
Institute of Biostructures and Bioimaging C.N.R. Napoli Italy
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33 (2), Moscow, Russian Federation
References:
Kaprelyants, A.S., Kell, D.B., Dormancy in stationary-phase cultures of Micrococcus luteus: Flow cytometric analysis of starvation and resuscitation (1993) Appl Environ Microbiol, 59, pp. 3187-319
Kana, B.D., Gordhan, B.G., Downing, K.J., Sung, N., Vostroktunova, G., Machowski, E.E., Tsenova, L., Kaplan, G., The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in vitro (2008) Mol Microbiol, 67, pp. 672-684
Kana, B.D., Mizrahi, V., Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling (2010) FEMS Immunol Med Microbiol, 58, pp. 39-50
Lillebaek, T., Dirksen, A., Baess, I., Strunge, B., Thomsen VØ., Andersen, A.B., Molecular evidence of endogenous reactivation of Mycobacterium tuberculosis after 33 years of latent infection (2002) J Infect Dis, 185, pp. 401-404
Wu, X., Yang, Y., Han, Y., Zhang, J., Liang, Y., Li, H., Li, B., Wang, L., Effect of recombinant Rv1009 protein on promoting the growth of Mycobacterium tuberculosis (2008) J Appl Microbiol, 105, pp. 1121-1127
Mukamolova, G.V., Turapov, O., Malkin, J., Woltmann, G., Barer, M.R., Resuscitation-promoting factors reveal an occult population of tubercle Bacilli in Sputum (2010) Am J Respir Crit Care Med, 181, pp. 174-180
Downing, K.J., Mischenko, V.V., Shleeva, M.O., Young, D.I., Young, M., Kaprelyants, A.S., Apt, A.S., Mizrahi, V., Mutants of Mycobacterium tuberculosis lacking three of the five rpf-like genes are defective for growth in vivo and for resuscitation in vitro (2005) Infect Immun, 73, pp. 3038-3043
Tufariello, J.M., Mi, K., Xu, J., Manabe, Y.C., Kesavan, A.K., Drumm, J., Tanaka, K., Chan, J., Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis (2006) Infect Immun, 74, pp. 2985-2995
Biketov, S., Potapov, V., Ganina, E., Downing, K., Kana, B.D., Kaprelyants, A., The role of resuscitation promoting factors in pathogenesis and reactivation of Mycobacterium tuberculosis during intra-peritoneal infection in mice (2007) BMC, 17, p. 146
Cohen-Gonsaud, M., Barthe, P., Bagnéris, C., Henderson, B., Ward, J., Roumestand, C., Keep, N.H., The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes (2005) Nat Struct Mol Biol, 12, pp. 270-273
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. Tuberculosis (2009) J Mol Biol, 385, pp. 153-162
Mukamolova, G.V., Murzin, A.G., Salina, E.G., Demina, G.R., Kell, D.B., Kaprelyants, A.S., Young, M., Muralytic activity of Micrococcus luteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation (2006) Mol Microbiol, 59, pp. 84-98
Telkov, M.V., Demina, G.R., Voloshin, S.A., Salina, E.G., Dudik, T.V., Stekhanova, T.N., Mukamolova, G.V., Young, M., Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycanhydrolases (2006) Biochemistry (Mosc), 71, pp. 414-422
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis (2013) J Biomol Struct Dyn, 31, pp. 195-205
Ruggiero, A., Squeglia, F., Esposito, C., Marasco, D., Pedone, E., Pedone, C., Berisio, R., Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M. Tuberculosis (2010) Protein Pept Lett, 17, pp. 70-73
Hett, E.C., Chao, M.C., Steyn, A.J., Fortune, S.M., Deng, L.L., Rubin, E.J., A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis (2007) Mol Microbiol, 66, pp. 658-668
Squeglia, F., Ruggiero, A., Romano, M., Vitagliano, L., Berisio, R., Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: Evidence for the L-to-D inversion of configuration of the catalytic cysteine (2014) Acta Crystallogr D Biol Crystallogr, 70, pp. 2295-2300
Brennan, P.J., Nikaido, H., The envelope of mycobacteria (1995) Annu Rev Biochem, 64, pp. 29-63
Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Mainardi, J.L., The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L D-transpeptidation (2008) J Bacteriol, 190, pp. 4360-4366
Vollmer, W., Höltje, J.V., The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)? (2004) J Bacteriol, 186, pp. 5978-5987
Brennan, P.J., Crick, D.C., The cell-wall core of Mycobacterium tuberculosis in the context of drug discovery (2007) Curr Top Med Chem, 7, pp. 475-488
Gupta, R., Lavollay, M., Mainardi, J.L., Arthur, M., Bishai, W.R., Lamichhane, G., The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin (2010) Nat Med, 16, pp. 466-469
Correale, S., Ruggiero, A., Capparelli, R., Pedone, E., Berisio, R., Structures of free and inhibited forms of the L, D-transpeptidase LdtMt1 from Mycobacterium tuberculosis (2013) Acta Crystallogr D Biol Crystallogr, 69, pp. 1697-1706
Priyadarshini, R., Popham, D.L., Young, K.D., Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli (2006) J Bacteriol, 188, pp. 5345-5355
Heidrich, C., Ursinus, A., Berger, J., Schwarz, H., Höltje, J.V., Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli (2002) J Bacteriol, 184, pp. 6093-6099
Nikitushkin, V.D., Demina, G.R., Shleeva, M.O., Kaprelyants, A.S., Peptidoglycan fragments stimulate resuscitation of "non-culturable" mycobacteria (2013) Antonie Van Leeuwenhoek, 103, pp. 37-46
Squeglia, F., Romano, M., Ruggiero, A., Vitagliano, L., De Simone, A., Berisio, R., Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses (2013) Biophys J, 104, pp. 2530-2539
Chao, M.C., Kieser, K.J., Minami, S., Mavrici, D., Aldridge, B.B., Fortune, S.M., Alber, T., Rubin, E.J., Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria (2013) PLoS Pathog, 9, p. e1003197
Shleeva, M., Mukamolova, G.V., Young, M., Williams, H.D., Kaprelyants, A.S., Formation of 'non-culturable' cells of Mycobacterium smegmatis in stationary phase in response to growth under suboptimal conditions and their Rpf-mediated resuscitation (2004) Microbiology, 150, pp. 1687-1697
Matsushima, Y., Miyazaki, T., Kasai, S., Chemical evidence for the Phillips model of the action of hen egg white lysozyme (1968) Nature, 219, p. 265
Vocadlo, D.J., Davies, G.J., Laine, R., Withers, S.G., Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate (2001) Nature, 412, pp. 835-838
Phillips, D.C., The hen egg white lysozyme molecule (1967) Proc Natl Acad Sci USA, 57, pp. 483-495
Höltje, J.V., Mirelman, D., Sharon, N., Schwarz, U., Novel type of murein transglycosylase in Escherichia coli (1975) J Bacteriol, 124, pp. 1067-1076
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments (2008) Cell, 135, pp. 486-496
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (2011) J Am Chem Soc, 133, pp. 20676-20679
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (2012) Curr Protein Pept Sci, 13, pp. 756-766
Lee, M., Hesek, D., Shah, I.M., Oliver, A.G., Dworkin, J., Mobashery, S., Synthetic peptidoglycan motifs for germination of bacterial spores (2010) ChemBioChem, 11, pp. 2525-2529
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G.J., Husson, R.N., The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization (2011) PLoS Pathog, 7, p. e1002182
Park, J.T., Uehara, T., How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan) (2008) Microbiol Mol Biol Rev, 72, pp. 211-227
Reith, J., Mayer, C., Peptidoglycanturnover and recycling in Gram-positive bacteria (2011) Appl Microbiol Biotechnol, 92, pp. 1-11
Höltje, J.V., Kopp, U., Ursinus, A., Wiedemann, B., The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase (1994) FEMS Microbiol Lett, 122, pp. 159-164
Prigozhin, D.M., Mavrici, D., Huizar, J.P., Vansell, H.J., Alber, T., Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-L-alanine amidase Rv3717 point to a role in peptidoglycanfragment recycling (2013) J Biol Chem, 288, pp. 31549-31555
Parish, T., Stocker, N., Methods in molecular Biology (1998) Mycobacteria Protocols, pp. 91-107. , Humana Press, Totowa, NJ
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (2010) Structure, 18, pp. 1184-1190
Rostovtseva, L., Andronova, T., Malkova, V., Sorokina, I., Ivaniv, V., Synthesis and antitumor activity of glycopeptides containing N-Acetylglucosaminil-(ß 1-4)-N-acetylmuramyl disaccharide unit (1981) Bioorg Khim, 12, pp. 1843-1858. , Russian
Hoshino, O., Zehavi, U., Sîna, P., Jeanloz, R.W., The isolation and structure identification of a discaccharide containing manno-muramic acid from Micrococcus lysodeikticus cell wall (1972) J Biol Chem, 247, pp. 381-390
Zemlyakov, A., Synthesis of γ-benzyl tert-butoxycarbonyl-L-alanyl-D-glutamate and its derivatives (1998) Chem Nat Compd, 34, pp. 78-79
Chun, Y., Yan, S., Li, X., Ding, N., Zhang, W., Wang, P., Li, M., Li, Y., Synthesis of 1,6-anhydro sugars catalyzed by silica supported perchloric acid (2011) Tetrahedron Lett, 52, pp. 6196-6198
A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria
Resuscitation promoting factor proteins (Rpfs) are known to participate in reactivating the dormant forms of actinobacteria. Structural analysis of the Rpf catalytic domain demonstrates its similarity to lysozyme and to lytic transglycosylases - the groups of enzymes that cleave the beta-1,4-glycosydic bond between N-acetylmuramic acid (N-AcMur) and N-acetylglucosamine (N-AcGlc) and concomitantly form a 1,6-anhydro ring at the N-AcMur residue. Analysis of the products formed from mycobacterial peptidoglycan hydrolysis reactions containing a mixture of RpfB and resuscitation promoting factor interacting protein (RipA) allowed us to identify the suggested product of their action - N-acetylglucosaminyl-beta(1-->4)-N-glycolyl-1,6-anhydromuramyl-L-alanyl-D-isoglut amate. To identify the role of this resulting product in resuscitation, we used a synthetic 1,6-anhydro disaccharide dipeptide and tested its ability to stimulate resuscitation using the dormant M. smegmatis model. It has been found that the disaccharide-dipeptide is the minimal structure capable of resuscitating the dormant mycobacterial cells over the concentration range of 9 - 100 ng/ml. The current study provides, therefore, the first insight into the molecular mechanism of resuscitation from dormancy involving a product of RpfB/RipA-mediated peptidoglycan cleavage. This article is protected by copyright. All rights reserved.
Resuscitation promoting factor proteins (Rpfs) are known to participate in reactivating the dormant forms of actinobacteria. Structural analysis of the Rpf catalytic domain demonstrates its similarity to lysozyme and to lytic transglycosylases - the groups of enzymes that cleave the beta-1,4-glycosydic bond between N-acetylmuramic acid (N-AcMur) and N-acetylglucosamine (N-AcGlc) and concomitantly form a 1,6-anhydro ring at the N-AcMur residue. Analysis of the products formed from mycobacterial peptidoglycan hydrolysis reactions containing a mixture of RpfB and resuscitation promoting factor interacting protein (RipA) allowed us to identify the suggested product of their action - N-acetylglucosaminyl-beta(1-->4)-N-glycolyl-1,6-anhydromuramyl-L-alanyl-D-isoglut amate. To identify the role of this resulting product in resuscitation, we used a synthetic 1,6-anhydro disaccharide dipeptide and tested its ability to stimulate resuscitation using the dormant M. smegmatis model. It has been found that the disaccharide-dipeptide is the minimal structure capable of resuscitating the dormant mycobacterial cells over the concentration range of 9 - 100 ng/ml. The current study provides, therefore, the first insight into the molecular mechanism of resuscitation from dormancy involving a product of RpfB/RipA-mediated peptidoglycan cleavage. This article is protected by copyright. All rights reserved.
A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria
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A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria
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Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2010 Sep 8; 18(9): 1184-1190.
Impact Factor: 6.337
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* Structural and Binding Properties of the Active Cell Wall Hydrolase RipA from M. tuberculosis, a Promising Biosensing Molecule for Early Warning Bacterial Detection (5 views)
Curr Med Chem (ISSN: 0929-8673linking), 2022; 29(24): 4282-4292.
Impact Factor: 4.74
View Export to BibTeX Export to EndNote
Squeglia F, Moreira M, Ruggiero A, Berisio R
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Impact Factor: 5.7
View Export to BibTeX Export to EndNote
Squeglia F, Ruggiero A, Berisio R
* Chemistry of Peptidoglycan in Mycobacterium tuberculosis Life Cycle: An off-the-wall Balance of Synthesis and Degradation (104 views)
Chemistry (ISSN: 0947-6539linking, 1521-3765electronic), 2018 Feb 21; 24 (11 ): 2533-2546.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Squeglia F, Ruggiero A, Berisio R
* Chemistry of Peptidoglycan in Mycobacterium tuberculosis life style: an off-the-wall balance of synthesis and degradation (479 views) (PDF 222 views)
Chemistry (ISSN: 1521-3765electronic, 0947-6539linking), 2018; 24: 2533-2546.
Impact Factor: 5.317
View Export to BibTeX Export to EndNote
Berisio R, Squeglia F, Ruggiero A
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Impact Factor: 3.469
View Export to BibTeX Export to EndNote
Dennehy R, RomanoM, Ruggiero A, Mohamed YF, Dignam SL, Mujica Troncoso C, Callaghan M, Valvano MA, Berisio R, Mcclean S
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Impact Factor: 4.41
View Export to BibTeX Export to EndNote
Dennehy R, Romano M, Ruggiero A, Troncoso CM, Fathy Y, Callaghan M, Valvano M, Berisio R, Mcclean S
* Peptidoglycan-associated lipoprotein is a virulence factor that is involved in host cell attachment of Burkholderia cepacia complex (224 views)
Cellular Microbiology, 2016; inpress: N/D-N/D.
Impact Factor: 4.46
View Export to BibTeX Export to EndNote
Pica A, Chi M-C, Chen Y-Y, D'Ischia M, Lin L-L, Merlino A
* The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies (417 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1864(2): 195-203.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Ruggiero A, Squeglia F, Romano M, Vitagliano L, De Simone A, Berisio R
* The structure of Resuscitation promoting factor B from M. tuberculosis reveals unexpected ubiquitin-like domains (328 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2015 Nov 5; 1860(2): 445-451.
Impact Factor: 4.864
View Export to BibTeX Export to EndNote
De Simone G, Di Fiore A, Capasso C, Supuran CT
* The zinc coordination pattern in the eta-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families (472 views)
Bioorg Med Chem Lett (ISSN: 0960-894x), 2015 Apr 1; 25(7): 1385-1389.
Impact Factor: 2.486
View Export to BibTeX Export to EndNote
Squeglia F, Ruggiero A, Berisio R
* Exit from mycobacterial dormancy: a structural perspective (520 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 Feb 9; 22(14): 1698-1709.
Impact Factor: 3.455
View Export to BibTeX Export to EndNote
Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
* Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (438 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Impact Factor: 5.158
View Export to BibTeX Export to EndNote
Ceruso M, Carta F, Osman SM, Alothman Z, Monti SM, Supuran CT
* Inhibition studies of bacterial, fungal and protozoan β-class carbonic anhydrases with Schiff bases incorporating sulfonamide moieties (367 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 0968-0896linking), 2015; 23(15): 4181-4187.
Impact Factor: 2.923
View Export to BibTeX Export to EndNote
Calvanese L, Falcigno L, Maglione C, Marasco D, Ruggiero A, Squeglia F, Berisio R, D'Auria G
* Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis (475 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014 Jul; 101(7): 712-719.
Impact Factor: 2.385
View Export to BibTeX Export to EndNote
Correale S, Ruggiero A, Capparelli R, Pedone E, Berisio R
* Structures of free and inhibited forms of the L, D-transpeptidase LdtMt1 from Mycobacterium tuberculosis (402 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Sep; 69(Pt9): 1697-1706.
Impact Factor: 7.232
View Export to BibTeX Export to EndNote
Correale S, Ruggiero A, Pedone E, Berisio R
* Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the l, d-transpeptidase LdtMt1 from Mycobacterium tuberculosis (428 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013 Mar 1; 69(3): 253-256.
Impact Factor: 0.568
View Export to BibTeX Export to EndNote
Ruggiero A, De Simone P, Smaldone G, Squeglia F, Berisio R
* Bacterial cell division regulation by Ser/Thr kinases: A structural perspective (581 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 756-766.
Impact Factor: 2.326
View Export to BibTeX Export to EndNote
Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (554 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
View Export to BibTeX Export to EndNote
Roviello GN, Roviello G, Musumeci D, Bucci EM, Pedone C
* Dakin-West reaction on 1-thyminyl acetic acid for the synthesis of 1, 3-bis(1-thyminyl)-2-propanone, a heteroaromatic compound with nucleopeptide-binding properties (439 views)
Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2012 Oct; 43(4): 1615-1623.
Impact Factor: 3.914
View Export to BibTeX Export to EndNote
Berisio R
* Editorial: cell processes in bacterial diseases (409 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1011-1012.
Impact Factor: 1.994
View Export to BibTeX Export to EndNote
De Simone G
* Editorial: Zinc Metallo-Enzymes As Target For Drug Design (443 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2012 Feb; 19(6): 820-1012.
Impact Factor: 4.07
View Export to BibTeX Export to EndNote
Castellano I, Merlino A
* γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (425 views)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Impact Factor: 5.615
View Export to BibTeX Export to EndNote
Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, Dworkin J, Petoukhov M, Molinaro A, Berisio R, Silipo A
* Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (371 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2011 Dec 28; 133(51): 20676-20679.
Impact Factor: 9.907
View Export to BibTeX Export to EndNote
Ruggiero A, Squeglia F, Marasco D, Marchetti R, Molinaro A, Berisio R
* X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus (586 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 33-41.
Impact Factor: 4.897
View Export to BibTeX Export to EndNote
Merlino A, Russo Krauss I, Castellano I, De Vendittis E, Rossi B, Conte M, Vergara A, Sica F
* Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis (543 views)
J Struct Biol (ISSN: 1047-8477, 1047-8477linking), 2010 Dec; 172(3): 343-352.
Impact Factor: 3.5
View Export to BibTeX Export to EndNote
Ruggiero A, Squeglia F, Izzo V, Silipo A, Vitagliano L, Molinaro A, Berisio R
* Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus (387 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Oct; 17(10): 1296-1299.
Impact Factor: 1.849
View Export to BibTeX Export to EndNote
Ruggiero A, Marasco D, Squeglia F, Soldini S, Pedone E, Pedone C, Berisio R
* Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (425 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2010 Sep 8; 18(9): 1184-1190.
Impact Factor: 6.337
View Export to BibTeX Export to EndNote
Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
* Crystal Structure of the Resuscitation-Promoting Factor (Delta DUF)RpfB from M. tuberculosis (597 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
View Export to BibTeX Export to EndNote
Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (236 views)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
View Export to BibTeX Export to EndNote
Prato S, Vitale RM, Contursi P, Lipps G, Saviano M, Rossi M, Bartolucci S
* Molecular modeling and functional characterization of the monomeric primase-polymerase domain from the Sulfolobus solfataricus plasmid pIT3 (402 views)
Febs J (ISSN: 1742-464x), 2008; 275(17): 4389-4402.
Impact Factor: 3.139
View Export to BibTeX Export to EndNote
Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (319 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus (545 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Dec 16; 42(49): 14397-14407.
Impact Factor: 3.922
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Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (458 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
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33 Records (33 excluding Abstracts).
Total impact factor: 140.642 (140.642 excluding Abstracts).
Total 5 year impact factor: 141.852 (141.852 excluding Abstracts).
Total impact factor: 140.642 (140.642 excluding Abstracts).
Total 5 year impact factor: 141.852 (141.852 excluding Abstracts).
491 views. Last view on Thursday 25 May 2023, 9:04:20
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