Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo (375 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2014 May 6; 22(5): 719-730.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.618, 5-year impact factor: 5.895
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84899892117&partnerID=40&md5=8f8402fcd2023c51024441736ea21ae2
Keywords: Adenine, Adenosine Phosphate, Exoribonuclease, Polyadenylic Acid, Uridine Phosphate, Article, Bacterial Virulence, Crystal Structure, Embryo, Enzyme Specificity, Enzyme Structure, Enzyme Substrate, Escherichia Coli, Hydrogen Bond, In Vivo Study, Maturation, Mycobacterium, Nonhuman, Priority Journal, Protein Family, Protein Function, Bacteria (microorganisms), Mycobacterium Tuberculosis,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Medical Microbiology and Infection Control, VU University Medical Center, Van der Boechorststraat 7, Amsterdam, 1081 BT, Netherlands
References:
Abdallah, A.M., Verboom, T., Hannes, F., Safi, M., Strong, M., Eisenberg, D., Musters, R.J., Bitter, W., A specific secretion system mediates PPE41 transport in pathogenic mycobacteria (2006) Mol. Microbiol., 62, pp. 667-67
Abe, M., Suzuki, H., Nishitsuji, H., Shida, H., Takaku, H., Interaction of human T-cell lymphotropic virus type i Rex protein with Dicer suppresses RNAi silencing (2010) FEBS Lett., 584, pp. 4313-4318
Abendroth, J., Ollodart, A., Andrews, E.S., Myler, P.J., Staker, B.L., Edwards, T.E., Arcus, V.L., Grundner, C., Mycobacterium tuberculosis Rv2179c protein establishes a new exoribonuclease family with broad phylogenetic distribution (2014) J. Biol. Chem., 289, pp. 2139-2147
Adilakshmi, T., Ayling, P.D., Ratledge, C., Polyadenylylation in mycobacteria: Evidence for oligo(dT)-primed cDNA synthesis (2000) Microbiology, 146, pp. 633-638
Alonso, H., Aguilo, J.I., Samper, S., Caminero, J.A., Campos-Herrero, M.I., Gicquel, B., Brosch, R., Otal, I., Deciphering the role of IS6110 in a highly transmissible Mycobacterium tuberculosis Beijing strain, GC1237 (2011) Tuberculosis (Edinb.), 91, pp. 117-126
Baba, O., Production of monoclonal antibody that recognizes glycogen and its application for immunohistochemistry (1993) Kokubyo Gakkai Zasshi, 60, pp. 264-287
Berisio, R., Editorial: Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (2012) Curr. Protein Pept. Sci., 13, pp. 697-698
Bouley, D.M., Ghori, N., Mercer, K.L., Falkow, S., Ramakrishnan, L., Dynamic nature of host-pathogen interactions in Mycobacterium marinum granulomas (2001) Infect. Immun., 69, pp. 7820-7831
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
Brennan, P.J., Nikaido, H., The envelope of mycobacteria (1995) Annu. Rev. Biochem., 64, pp. 29-63
Broussard, G.W., Ennis, D.G., Mycobacterium marinum produces long-term chronic infections in medaka: A new animal model for studying human tuberculosis (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol., 145, pp. 45-54
Chan, K., Knaak, T., Satkamp, L., Humbert, O., Falkow, S., Ramakrishnan, L., Complex pattern of Mycobacterium marinum gene expression during long-term granulomatous infection (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 3920-3925
Chao, M.C., Rubin, E.J., Letting sleeping dos lie: Does dormancy play a role in tuberculosis? (2010) Annu. Rev. Microbiol., 64, pp. 293-311
Cheng, T.J., Sung, M.T., Liao, H.Y., Chang, Y.F., Chen, C.W., Huang, C.Y., Chou, L.Y., Cheng, Y.S., Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 431-436
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
Cywes, C., Hoppe, H.C., Daffé, M., Ehlers, M.R., Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent (1997) Infect. Immun., 65, pp. 4258-4266
Daffé, M., Etienne, G., The capsule of Mycobacterium tuberculosis and its implications for pathogenicity (1999) Tuber. Lung Dis., 79, pp. 153-169
Ehlers, M.R., Daffé, M., Interactions between Mycobacterium tuberculosis and host cells: Are mycobacterial sugars the key? (1998) Trends Microbiol., 6, pp. 328-335
Esposito, C., Pethoukov, M.V., Svergun, D.I., Ruggiero, A., Pedone, C., Pedone, E., Berisio, R., Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (2008) J. Bacteriol., 190, pp. 4749-4753
Gagliardi, M.C., Lemassu, A., Teloni, R., Mariotti, S., Sargentini, V., Pardini, M., Daffé, M., Nisini, R., Cell wall-associated alpha-glucan is instrumental for Mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte (2007) Cell. Microbiol., 9, pp. 2081-2092
Geurtsen, J., Chedammi, S., Mesters, J., Cot, M., Driessen, N.N., Sambou, T., Kakutani, R., Takata, H., Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: Involvement of mycobacterial capsular polysaccharides in host immune modulation (2009) J. Immunol., 183, pp. 5221-5231
Goldenberg, O., Erez, E., Nimrod, G., Ben-Tal, N., The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures (2009) Nucleic Acids Res., 37, pp. 323-D327
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., Engelhardt, H., Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 3963-3967
Hsiao, Y.Y., Yang, C.C., Lin, C.L., Lin, J.L., Duh, Y., Yuan, H.S., Structural basis for RNA trimming by RNase T in stable RNA 3′-end maturation (2011) Nat. Chem. Biol., 7, pp. 236-243
Hsiao, Y.Y., Duh, Y., Chen, Y.P., Wang, Y.T., Yuan, H.S., How an exonuclease decides where to stop in trimming of nucleic acids: Crystal structures of RNase T-product complexes (2012) Nucleic Acids Res., 40, pp. 8144-8154
Kaur, D., Berg, S., Dinadayala, P., Gicquel, B., Chatterjee, D., McNeil, M.R., Vissa, V.D., Brennan, P.J., Biosynthesis of mycobacterial lipoarabinomannan: Role of a branching mannosyltransferase (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 13664-13669
Kaur, D., Obregón-Henao, A., Pham, H., Chatterjee, D., Brennan, P.J., Jackson, M., Lipoarabinomannan of Mycobacterium: Mannose capping by a multifunctional terminal mannosyltransferase (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 17973-17977
Langer, G., Cohen, S.X., Lamzin, V.S., Perrakis, A., Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 (2008) Nat. Protoc., 3, pp. 1171-1179
Lemassu, A., Daffé, M., Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis (1994) Biochem. J., 297, pp. 351-357
Mishra, A.K., Krumbach, K., Rittmann, D., Appelmelk, B., Pathak, V., Pathak, A.K., Nigou, J., Besra, G.S., Lipoarabinomannan biosynthesis in Corynebacterineae: The interplay of two α(1→2)-mannopyranosyltransferases MptC and MptD in mannan branching (2011) Mol. Microbiol., 80, pp. 1241-1259
Mohanty, B.K., Kushner, S.R., Deregulation of poly(A) polymerase i in Escherichia coli inhibits protein synthesis and leads to cell death (2013) Nucleic Acids Res., 41, pp. 1757-1766
Mohanty, B.K., Maples, V.F., Kushner, S.R., Polyadenylation helps regulate functional tRNA levels in Escherichia coli (2012) Nucleic Acids Res., 40, pp. 4589-4603
Ortalo-Magné, A., Dupont, M.A., Lemassu, A., Andersen, A.B., Gounon, P., Daffé, M., Molecular composition of the outermost capsular material of the tubercle bacillus (1995) Microbiology, 141, pp. 1609-1620
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Sambou, T., Dinadayala, P., Stadthagen, G., Barilone, N., Bordat, Y., Constant, P., Levillain, F., Lemassu, A., Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: Biosynthesis and impact on the persistence in mice (2008) Mol. Microbiol., 70, pp. 762-774
Sani, M., Houben, E.N., Geurtsen, J., Pierson, J., De Punder, K., Van Zon, M., Wever, B., Daffé, M., Direct visualization by cryo-EM of the mycobacterial capsular layer: A labile structure containing ESX-1-secreted proteins (2010) PLoS Pathog., 6, p. 1000794
Sassetti, C.M., Boyd, D.H., Rubin, E.J., Genes required for mycobacterial growth defined by high density mutagenesis (2003) Mol. Microbiol., 48, pp. 77-84
Sheldrick, G.M., A short history of SHELX (2008) Acta Crystallogr. A, 64, pp. 112-122
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
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
Squeglia, F., Bachert, B., De Simone, A., Lukomski, S., Berisio, R., The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A streptococcus shows significant similarity to immunomodulatory HIV protein gp41 (2014) J. Biol. Chem., 289, pp. 5122-5133
Stokes, R.W., Norris-Jones, R., Brooks, D.E., Beveridge, T.J., Doxsee, D., Thorson, L.M., The glycan-rich outer layer of the cell wall of Mycobacterium tuberculosis acts as an antiphagocytic capsule limiting the association of the bacterium with macrophages (2004) Infect. Immun., 72, pp. 5676-5686
Stoop, E.J., Schipper, T., Huber, S.K., Nezhinsky, A.E., Verbeek, F.J., Gurcha, S.S., Besra, G.S., Van Der Sar, A.M., Zebrafish embryo screen for mycobacterial genes involved in the initiation of granuloma formation reveals a newly identified ESX-1 component (2011) Dis. Model. Mech., 4, pp. 526-536
Stoop, E.J., Mishra, A.K., Driessen, N.N., Van Stempvoort, G., Bouchier, P., Verboom, T., Van Leeuwen, L.M., Van Zon, M., Mannan core branching of lipo(arabino)mannan is required for mycobacterial virulence in the context of innate immunity (2013) Cell. Microbiol., 15, pp. 2093-2108
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Van Der Sar, A.M., Abdallah, A.M., Sparrius, M., Reinders, E., Vandenbroucke-Grauls, C.M., Bitter, W., Mycobacterium marinum strains can be divided into two distinct types based on genetic diversity and virulence (2004) Infect. Immun., 72, pp. 6306-6312
Van Hoof, A., Lennertz, P., Parker, R., Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast (2000) EMBO J., 19, pp. 1357-1365
Yoda, M., Cifuentes, D., Izumi, N., Sakaguchi, Y., Suzuki, T., Giraldez, A.J., Tomari, Y., Poly(A)-specific ribonuclease mediates 3′-end trimming of Argonaute2-cleaved precursor microRNAs (2013) Cell Rep., 5, pp. 715-726
Zuo, Y., Deutscher, M.P., Mechanism of action of RNase T. I. Identification of residues required for catalysis, substrate binding, and dimerization (2002) J. Biol. Chem., 277, pp. 50155-50159
Zuo, Y., Wang, Y., Malhotra, A., Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing (2005) Structure, 13, pp. 973-984
Zuo, Y., Zheng, H., Wang, Y., Chruszcz, M., Cymborowski, M., Skarina, T., Savchenko, A., Minor, W., Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover (2007) Structure, 15, pp. 417-428
Abdallah, A. M., Verboom, T., Hannes, F., Safi, M., Strong, M., Eisenberg, D., Musters, R. J., Bitter, W., A specific secretion system mediates PPE41 transport in pathogenic mycobacteria (2006) Mol. Microbiol., 62, pp. 667-67
Bouley, D. M., Ghori, N., Mercer, K. L., Falkow, S., Ramakrishnan, L., Dynamic nature of host-pathogen interactions in Mycobacterium marinum granulomas (2001) Infect. Immun., 69, pp. 7820-7831
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
Brennan, P. J., Nikaido, H., The envelope of mycobacteria (1995) Annu. Rev. Biochem., 64, pp. 29-63
Broussard, G. W., Ennis, D. G., Mycobacterium marinum produces long-term chronic infections in medaka: A new animal model for studying human tuberculosis (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol., 145, pp. 45-54
Chao, M. C., Rubin, E. J., Letting sleeping dos lie: Does dormancy play a role in tuberculosis? (2010) Annu. Rev. Microbiol., 64, pp. 293-311
Cheng, T. J., Sung, M. T., Liao, H. Y., Chang, Y. F., Chen, C. W., Huang, C. Y., Chou, L. Y., Cheng, Y. S., Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 431-436
Daff, M., Etienne, G., The capsule of Mycobacterium tuberculosis and its implications for pathogenicity (1999) Tuber. Lung Dis., 79, pp. 153-169
Ehlers, M. R., Daff, M., Interactions between Mycobacterium tuberculosis and host cells: Are mycobacterial sugars the key? (1998) Trends Microbiol., 6, pp. 328-335
Gagliardi, M. C., Lemassu, A., Teloni, R., Mariotti, S., Sargentini, V., Pardini, M., Daff, M., Nisini, R., Cell wall-associated alpha-glucan is instrumental for Mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte (2007) Cell. Microbiol., 9, pp. 2081-2092
Hett, E. C., Rubin, E. J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
Hsiao, Y. Y., Yang, C. C., Lin, C. L., Lin, J. L., Duh, Y., Yuan, H. S., Structural basis for RNA trimming by RNase T in stable RNA 3 -end maturation (2011) Nat. Chem. Biol., 7, pp. 236-243
Hsiao, Y. Y., Duh, Y., Chen, Y. P., Wang, Y. T., Yuan, H. S., How an exonuclease decides where to stop in trimming of nucleic acids: Crystal structures of RNase T-product complexes (2012) Nucleic Acids Res., 40, pp. 8144-8154
Kaur, D., Obreg n-Henao, A., Pham, H., Chatterjee, D., Brennan, P. J., Jackson, M., Lipoarabinomannan of Mycobacterium: Mannose capping by a multifunctional terminal mannosyltransferase (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 17973-17977
Lemassu, A., Daff, M., Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis (1994) Biochem. J., 297, pp. 351-357
Mishra, A. K., Krumbach, K., Rittmann, D., Appelmelk, B., Pathak, V., Pathak, A. K., Nigou, J., Besra, G. S., Lipoarabinomannan biosynthesis in Corynebacterineae: The interplay of two (1 2) -mannopyranosyltransferases MptC and MptD in mannan branching (2011) Mol. Microbiol., 80, pp. 1241-1259
Mohanty, B. K., Kushner, S. R., Deregulation of poly (A) polymerase i in Escherichia coli inhibits protein synthesis and leads to cell death (2013) Nucleic Acids Res., 41, pp. 1757-1766
Mohanty, B. K., Maples, V. F., Kushner, S. R., Polyadenylation helps regulate functional tRNA levels in Escherichia coli (2012) Nucleic Acids Res., 40, pp. 4589-4603
Ortalo-Magn, A., Dupont, M. A., Lemassu, A., Andersen, A. B., Gounon, P., Daff, M., Molecular composition of the outermost capsular material of the tubercle bacillus (1995) Microbiology, 141, pp. 1609-1620
Sassetti, C. M., Boyd, D. H., Rubin, E. J., Genes required for mycobacterial growth defined by high density mutagenesis (2003) Mol. Microbiol., 48, pp. 77-84
Sheldrick, G. M., A short history of SHELX (2008) Acta Crystallogr. A, 64, pp. 112-122
Stokes, R. W., Norris-Jones, R., Brooks, D. E., Beveridge, T. J., Doxsee, D., Thorson, L. M., The glycan-rich outer layer of the cell wall of Mycobacterium tuberculosis acts as an antiphagocytic capsule limiting the association of the bacterium with macrophages (2004) Infect. Immun., 72, pp. 5676-5686
Stoop, E. J., Schipper, T., Huber, S. K., Nezhinsky, A. E., Verbeek, F. J., Gurcha, S. S., Besra, G. S., Van Der Sar, A. M., Zebrafish embryo screen for mycobacterial genes involved in the initiation of granuloma formation reveals a newly identified ESX-1 component (2011) Dis. Model. Mech., 4, pp. 526-536
Stoop, E. J., Mishra, A. K., Driessen, N. N., Van Stempvoort, G., Bouchier, P., Verboom, T., Van Leeuwen, L. M., Van Zon, M., Mannan core branching of lipo (arabino) mannan is required for mycobacterial virulence in the context of innate immunity (2013) Cell. Microbiol., 15, pp. 2093-2108
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2014 May 6; 22(5): 719-730.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.618, 5-year impact factor: 5.895
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84899892117&partnerID=40&md5=8f8402fcd2023c51024441736ea21ae2
Keywords: Adenine, Adenosine Phosphate, Exoribonuclease, Polyadenylic Acid, Uridine Phosphate, Article, Bacterial Virulence, Crystal Structure, Embryo, Enzyme Specificity, Enzyme Structure, Enzyme Substrate, Escherichia Coli, Hydrogen Bond, In Vivo Study, Maturation, Mycobacterium, Nonhuman, Priority Journal, Protein Family, Protein Function, Bacteria (microorganisms), Mycobacterium Tuberculosis,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Medical Microbiology and Infection Control, VU University Medical Center, Van der Boechorststraat 7, Amsterdam, 1081 BT, Netherlands
References:
Abdallah, A.M., Verboom, T., Hannes, F., Safi, M., Strong, M., Eisenberg, D., Musters, R.J., Bitter, W., A specific secretion system mediates PPE41 transport in pathogenic mycobacteria (2006) Mol. Microbiol., 62, pp. 667-67
Abe, M., Suzuki, H., Nishitsuji, H., Shida, H., Takaku, H., Interaction of human T-cell lymphotropic virus type i Rex protein with Dicer suppresses RNAi silencing (2010) FEBS Lett., 584, pp. 4313-4318
Abendroth, J., Ollodart, A., Andrews, E.S., Myler, P.J., Staker, B.L., Edwards, T.E., Arcus, V.L., Grundner, C., Mycobacterium tuberculosis Rv2179c protein establishes a new exoribonuclease family with broad phylogenetic distribution (2014) J. Biol. Chem., 289, pp. 2139-2147
Adilakshmi, T., Ayling, P.D., Ratledge, C., Polyadenylylation in mycobacteria: Evidence for oligo(dT)-primed cDNA synthesis (2000) Microbiology, 146, pp. 633-638
Alonso, H., Aguilo, J.I., Samper, S., Caminero, J.A., Campos-Herrero, M.I., Gicquel, B., Brosch, R., Otal, I., Deciphering the role of IS6110 in a highly transmissible Mycobacterium tuberculosis Beijing strain, GC1237 (2011) Tuberculosis (Edinb.), 91, pp. 117-126
Baba, O., Production of monoclonal antibody that recognizes glycogen and its application for immunohistochemistry (1993) Kokubyo Gakkai Zasshi, 60, pp. 264-287
Berisio, R., Editorial: Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (2012) Curr. Protein Pept. Sci., 13, pp. 697-698
Bouley, D.M., Ghori, N., Mercer, K.L., Falkow, S., Ramakrishnan, L., Dynamic nature of host-pathogen interactions in Mycobacterium marinum granulomas (2001) Infect. Immun., 69, pp. 7820-7831
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
Brennan, P.J., Nikaido, H., The envelope of mycobacteria (1995) Annu. Rev. Biochem., 64, pp. 29-63
Broussard, G.W., Ennis, D.G., Mycobacterium marinum produces long-term chronic infections in medaka: A new animal model for studying human tuberculosis (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol., 145, pp. 45-54
Chan, K., Knaak, T., Satkamp, L., Humbert, O., Falkow, S., Ramakrishnan, L., Complex pattern of Mycobacterium marinum gene expression during long-term granulomatous infection (2002) Proc. Natl. Acad. Sci. USA, 99, pp. 3920-3925
Chao, M.C., Rubin, E.J., Letting sleeping dos lie: Does dormancy play a role in tuberculosis? (2010) Annu. Rev. Microbiol., 64, pp. 293-311
Cheng, T.J., Sung, M.T., Liao, H.Y., Chang, Y.F., Chen, C.W., Huang, C.Y., Chou, L.Y., Cheng, Y.S., Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 431-436
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
Cywes, C., Hoppe, H.C., Daffé, M., Ehlers, M.R., Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent (1997) Infect. Immun., 65, pp. 4258-4266
Daffé, M., Etienne, G., The capsule of Mycobacterium tuberculosis and its implications for pathogenicity (1999) Tuber. Lung Dis., 79, pp. 153-169
Ehlers, M.R., Daffé, M., Interactions between Mycobacterium tuberculosis and host cells: Are mycobacterial sugars the key? (1998) Trends Microbiol., 6, pp. 328-335
Esposito, C., Pethoukov, M.V., Svergun, D.I., Ruggiero, A., Pedone, C., Pedone, E., Berisio, R., Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (2008) J. Bacteriol., 190, pp. 4749-4753
Gagliardi, M.C., Lemassu, A., Teloni, R., Mariotti, S., Sargentini, V., Pardini, M., Daffé, M., Nisini, R., Cell wall-associated alpha-glucan is instrumental for Mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte (2007) Cell. Microbiol., 9, pp. 2081-2092
Geurtsen, J., Chedammi, S., Mesters, J., Cot, M., Driessen, N.N., Sambou, T., Kakutani, R., Takata, H., Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: Involvement of mycobacterial capsular polysaccharides in host immune modulation (2009) J. Immunol., 183, pp. 5221-5231
Goldenberg, O., Erez, E., Nimrod, G., Ben-Tal, N., The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures (2009) Nucleic Acids Res., 37, pp. 323-D327
Hett, E.C., Rubin, E.J., Bacterial growth and cell division: A mycobacterial perspective (2008) Microbiol. Mol. Biol. Rev., 72, pp. 126-156
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., Engelhardt, H., Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 3963-3967
Hsiao, Y.Y., Yang, C.C., Lin, C.L., Lin, J.L., Duh, Y., Yuan, H.S., Structural basis for RNA trimming by RNase T in stable RNA 3′-end maturation (2011) Nat. Chem. Biol., 7, pp. 236-243
Hsiao, Y.Y., Duh, Y., Chen, Y.P., Wang, Y.T., Yuan, H.S., How an exonuclease decides where to stop in trimming of nucleic acids: Crystal structures of RNase T-product complexes (2012) Nucleic Acids Res., 40, pp. 8144-8154
Kaur, D., Berg, S., Dinadayala, P., Gicquel, B., Chatterjee, D., McNeil, M.R., Vissa, V.D., Brennan, P.J., Biosynthesis of mycobacterial lipoarabinomannan: Role of a branching mannosyltransferase (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 13664-13669
Kaur, D., Obregón-Henao, A., Pham, H., Chatterjee, D., Brennan, P.J., Jackson, M., Lipoarabinomannan of Mycobacterium: Mannose capping by a multifunctional terminal mannosyltransferase (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 17973-17977
Langer, G., Cohen, S.X., Lamzin, V.S., Perrakis, A., Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 (2008) Nat. Protoc., 3, pp. 1171-1179
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Mohanty, B. K., Maples, V. F., Kushner, S. R., Polyadenylation helps regulate functional tRNA levels in Escherichia coli (2012) Nucleic Acids Res., 40, pp. 4589-4603
Ortalo-Magn, A., Dupont, M. A., Lemassu, A., Andersen, A. B., Gounon, P., Daff, M., Molecular composition of the outermost capsular material of the tubercle bacillus (1995) Microbiology, 141, pp. 1609-1620
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Sheldrick, G. M., A short history of SHELX (2008) Acta Crystallogr. A, 64, pp. 112-122
Stokes, R. W., Norris-Jones, R., Brooks, D. E., Beveridge, T. J., Doxsee, D., Thorson, L. M., The glycan-rich outer layer of the cell wall of Mycobacterium tuberculosis acts as an antiphagocytic capsule limiting the association of the bacterium with macrophages (2004) Infect. Immun., 72, pp. 5676-5686
Stoop, E. J., Schipper, T., Huber, S. K., Nezhinsky, A. E., Verbeek, F. J., Gurcha, S. S., Besra, G. S., Van Der Sar, A. M., Zebrafish embryo screen for mycobacterial genes involved in the initiation of granuloma formation reveals a newly identified ESX-1 component (2011) Dis. Model. Mech., 4, pp. 526-536
Stoop, E. J., Mishra, A. K., Driessen, N. N., Van Stempvoort, G., Bouchier, P., Verboom, T., Van Leeuwen, L. M., Van Zon, M., Mannan core branching of lipo (arabino) mannan is required for mycobacterial virulence in the context of innate immunity (2013) Cell. Microbiol., 15, pp. 2093-2108
Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo
The cell-envelope of Mycobacterium tuberculosis plays a key role in bacterial virulence and antibiotic resistance. Little is known about the molecular mechanisms of regulation of cell-envelope formation. Here, we elucidate functional and structural properties of RNase AS, which modulates M. tuberculosis cell-envelope properties and strongly impacts bacterial virulence in vivo. The structure of RNase AS reveals a resemblance to RNase T from Escherichia coli, an RNase of the DEDD family involved in RNA maturation. We show that RNase AS acts as a 3′-5′-exoribonuclease that specifically hydrolyzes adenylate-containing RNA sequences. Also, crystal structures of complexes with AMP and UMP reveal the structural basis for the observed enzyme specificity. Notably, RNase AS shows a mechanism of substrate recruitment, based on the recognition of the hydrogen bond donor NH2 group of adenine. Our work opens a field for the design of drugs able to reduce bacterial virulence in vivo. © 2014 Elsevier Ltd.
The cell-envelope of Mycobacterium tuberculosis plays a key role in bacterial virulence and antibiotic resistance. Little is known about the molecular mechanisms of regulation of cell-envelope formation. Here, we elucidate functional and structural properties of RNase AS, which modulates M. tuberculosis cell-envelope properties and strongly impacts bacterial virulence in vivo. The structure of RNase AS reveals a resemblance to RNase T from Escherichia coli, an RNase of the DEDD family involved in RNA maturation. We show that RNase AS acts as a 3′-5′-exoribonuclease that specifically hydrolyzes adenylate-containing RNA sequences. Also, crystal structures of complexes with AMP and UMP reveal the structural basis for the observed enzyme specificity. Notably, RNase AS shows a mechanism of substrate recruitment, based on the recognition of the hydrogen bond donor NH2 group of adenine. Our work opens a field for the design of drugs able to reduce bacterial virulence in vivo. © 2014 Elsevier Ltd.
Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo
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Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo
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Romano M, Ruggiero A, Squeglia F, Maga G, Berisio R
* A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping (491 views)
Cells (ISSN: 2073-4409linking, 2073-4409electronic), 2020 May 20; 9(5): 1297-1297.
Impact Factor: 6.6
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Calvanese L, Squeglia F, Romano M, D'Auria G, Falcigno L, Berisio R
* Structural and dynamic studies provide insights into specificity and allosteric regulation of Ribonuclease AS, a key enzyme in mycobacterial virulence (216 views) (PDF 10 views)
J Biomol Struct Dyn (ISSN: 0739-1102linking, 1538-0254electronic), 2020; N/D: 1-19.
Impact Factor: 3.11
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Roviello GN
* Novel insights into nucleoamino acids: biomolecular recognition and aggregation studies of a thymine-conjugated L-phenyl alanine (379 views)
Amino Acids (ISSN: 1438-2199electronic, 0939-4451linking), 2018 May 15; DOI10.1007/s00726-01: 933-941.
Impact Factor: 3.173
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Musumeci D, Roviello V, Roviello GN
* DNA- and RNA-binding ability of oligoDapT, a nucleobase-decorated peptide, for biomedical applications (1959 views)
Int J Nanomed (ISSN: 1176-9114linking, 1178-2013electronic), 2018 May 1; 2018:13: 2613-2629.
Impact Factor: 4.3
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Romano M, Squeglia F, Berisio R
* Structure and Function of RNase AS, a Novel Virulence Factor from Mycobacterium Tuberculosis (405 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 Apr 17; 22(14): 1745-1756.
Impact Factor: 3.455
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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
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Kaprelyants AS, Mukamolova GV, Ruggiero A, Makarov VA, Demina GR, Shleeva MO, Potapov VD, Shramko PA
* Resuscitation-promoting Factors (Rpf): In Search of Inhibitors (503 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1026-1034.
Impact Factor: 1.994
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Improta R, Barone V
* Interplay between "neutral" and "charge-transfer" excimers rules the excited state decay in adenine-rich polynucleotides (499 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2011 Dec 9; 50(50): 12016-12019.
Impact Factor: 13.455
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Esposito C, Pethoukov MV, Svergun DI, Ruggiero A, Pedone C, Pedone E, Berisio R
* Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (475 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2008 Jul; 190(13): 4749-4753.
Impact Factor: 3.636
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Chambery A, Pisante M, Di Maro A, Di Zazzo E, Ruvo M, Costantini S, Colonna G, Parente A
* Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (364 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Impact Factor: 3.354
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De Falco S, Ruvoletto MG, Verdoliva A, Ruvo M, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
* Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells (628 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
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Sandomenico A, Ruggiero A, Iaccarino E, Oliver A, Squeglia F, Moreira M, Esposito L, Ruvo M, Berisio R
Unveiling CD59-Antibody Interactions to Design Paratope-Mimicking Peptides for Complement Modulation (2 views)
Int J Mol Sci (ISSN: 1422-0067linking), N/D; 21222223241031126119: 500-519.
Impact Factor: 6.21
View Export to BibTeX Export to EndNote
* A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping (491 views)
Cells (ISSN: 2073-4409linking, 2073-4409electronic), 2020 May 20; 9(5): 1297-1297.
Impact Factor: 6.6
View Export to BibTeX Export to EndNote
Calvanese L, Squeglia F, Romano M, D'Auria G, Falcigno L, Berisio R
* Structural and dynamic studies provide insights into specificity and allosteric regulation of Ribonuclease AS, a key enzyme in mycobacterial virulence (216 views) (PDF 10 views)
J Biomol Struct Dyn (ISSN: 0739-1102linking, 1538-0254electronic), 2020; N/D: 1-19.
Impact Factor: 3.11
View Export to BibTeX Export to EndNote
Roviello GN
* Novel insights into nucleoamino acids: biomolecular recognition and aggregation studies of a thymine-conjugated L-phenyl alanine (379 views)
Amino Acids (ISSN: 1438-2199electronic, 0939-4451linking), 2018 May 15; DOI10.1007/s00726-01: 933-941.
Impact Factor: 3.173
View Export to BibTeX Export to EndNote
Musumeci D, Roviello V, Roviello GN
* DNA- and RNA-binding ability of oligoDapT, a nucleobase-decorated peptide, for biomedical applications (1959 views)
Int J Nanomed (ISSN: 1176-9114linking, 1178-2013electronic), 2018 May 1; 2018:13: 2613-2629.
Impact Factor: 4.3
View Export to BibTeX Export to EndNote
Romano M, Squeglia F, Berisio R
* Structure and Function of RNase AS, a Novel Virulence Factor from Mycobacterium Tuberculosis (405 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 Apr 17; 22(14): 1745-1756.
Impact Factor: 3.455
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
Kaprelyants AS, Mukamolova GV, Ruggiero A, Makarov VA, Demina GR, Shleeva MO, Potapov VD, Shramko PA
* Resuscitation-promoting Factors (Rpf): In Search of Inhibitors (503 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Oct; 19(10): 1026-1034.
Impact Factor: 1.994
View Export to BibTeX Export to EndNote
Improta R, Barone V
* Interplay between "neutral" and "charge-transfer" excimers rules the excited state decay in adenine-rich polynucleotides (499 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2011 Dec 9; 50(50): 12016-12019.
Impact Factor: 13.455
View Export to BibTeX Export to EndNote
Esposito C, Pethoukov MV, Svergun DI, Ruggiero A, Pedone C, Pedone E, Berisio R
* Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis (475 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2008 Jul; 190(13): 4749-4753.
Impact Factor: 3.636
View Export to BibTeX Export to EndNote
Chambery A, Pisante M, Di Maro A, Di Zazzo E, Ruvo M, Costantini S, Colonna G, Parente A
* Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (364 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Impact Factor: 3.354
View Export to BibTeX Export to EndNote
De Falco S, Ruvoletto MG, Verdoliva A, Ruvo M, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
* Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells (628 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
View Export to BibTeX Export to EndNote
Sandomenico A, Ruggiero A, Iaccarino E, Oliver A, Squeglia F, Moreira M, Esposito L, Ruvo M, Berisio R
Unveiling CD59-Antibody Interactions to Design Paratope-Mimicking Peptides for Complement Modulation (2 views)
Int J Mol Sci (ISSN: 1422-0067linking), N/D; 21222223241031126119: 500-519.
Impact Factor: 6.21
View Export to BibTeX Export to EndNote
12 Records (12 excluding Abstracts).
Total impact factor: 58.871 (58.871 excluding Abstracts).
Total 5 year impact factor: 57.447 (57.447 excluding Abstracts).
Total impact factor: 58.871 (58.871 excluding Abstracts).
Total 5 year impact factor: 57.447 (57.447 excluding Abstracts).
375 views. Last view on Thursday 09 March 2023, 21:57:13
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