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.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 9.907, 5-year impact factor: 9.766
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84555178075&partnerID=40&md5=1385a115e0ceea89e17d6e3defc8f053
Keywords: Arginine Residue, Bacillus Subtilis, Bacterial Spore, Cell Walls, Cellular Process, Extracellular Region, Growing Conditions, Molecular Signals, Muropeptides, Nmr Techniques, Peptidoglycans, Protein Mutagenesis, Structural Requirements, Bacteriology, Resuscitation, Walls (structural Partitions), Enzymes, Amino Acid Derivative, Bacterial Enzyme, Diaminopimelic Acid, Prkc Protein, Protein Serine Threonine Kinase, Unclassified Drug, Article, Bacterial Cell Wall, Bacterial Growth, Bacterial Survival, Binding Site, Carbohydrate Analysis, Carboxy Terminal Sequence, Cell Growth, Circular Dichroism, Controlled Study, Dormancy, Enzyme Binding, Extracellular Space, Germination, In Vitro Study, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Protein Domain, Protein Interaction, Protein Structure, Signal Transduction, Staphylococcus Aureus, Models, Mutation, Biomolecular, Protein Binding, Protein Conformation, Tertiary, Protein-Serine-Threonine Kinases, Substrate Specificity,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, Consiglio Nazionale Delle Ricerche (CNR), Via Mezzocannone 16, I-80134 Napoli, Italy
Department of Organic and Biological Chemistry, University of Naples Federico II, Via Cinthia 4, I-80126 Napoli, Italy
Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, United States
European Molecular Biology Laboratory, Hamburg Outstation, C/o DESY, Notkestrasse 85, 22607 Hamburg, Germany
References:
Hendrickx, A.P., Budzik, J.M., Oh, S.Y., Schneewind, O., (2011) Nat. Rev. Microbiol., 9, p. 16
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., (2009) J. Mol. Biol., 385, p. 153
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., (2010) Structure, 18, p. 1184
Kaprelyants, A.S., Mukamolova, G.V., Ruggiero, A., Makarov, V.A., Demina, G.R., Shleeva, M.O., Potapov, V.D., Shramko, P., (2011) Protein Pept. Lett., , not supplied
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., (2008) Cell, 135, p. 486
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., (2002) Mol. Microbiol., 46, p. 571
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., (2008) J. Biol. Chem., 283, p. 18099
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., (2003) J. Mol. Biol., 330, p. 459
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., (2009) Microbiology, 155, p. 932
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., (2011) Biochem. J., 435, p. 33
Meyer, B., Peters, T., (2003) Angew. Chem., Int. Ed., 42, p. 864
Angulo, J., Langpap, B., Blume, A., Biet, T., Meyer, B., Krishna, N.R.H., Peters, H., Peters, T., (2006) J. Am. Chem. Soc., 128, p. 13529
Roldos, V., Canada, F.J., Jimenez-Barbero, J., (2011) ChemBioChem, 12, p. 990
Mari, S., Serrano-Gomez, D., Canada, F.J., Corbi, A.L., Jimenez-Barbero, J., (2004) Angew. Chem., Int. Ed., 44, p. 296
Mayer, M., Meyer, B., (2001) J. Am. Chem. Soc., 123, p. 6108
Hu, X., Zhang, W., Carmichael, I., Serianni, A., (2010) J. Am. Chem. Soc., 132, p. 4641
Mieczkowski, C., Iavarone, A.T., Alber, T., (2008) EMBO J., 27, p. 3186
Debarbouille, M., Dramsi, S., Dussurget, O., Nahori, M.A., Vaganay, E., Jouvion, G., Cozzone, A., Duclos, B., (2009) J. Bacteriol., 191, p. 4070
Lim, J.H., Kim, M.S., Kim, H.E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W.E., Oh, B.H., (2006) J. Biol. Chem., 281, p. 8286
Mushtaq, M., Asong, J., Li, X., Cardot, J., Boons, G.-J., Husson, R.N., (2011) PLOS Pathog., 7, pp. e1002182
Schlessinger, J., Plotnikov, A.N., Ibrahimi, O.A., Eliseenkova, A.V., Yeh, B.K., Yayon, A., Linhardt, R.J., Mohammadi, M., (2000) Mol. Cell, 6, p. 743
Hendrickx, A. P., Budzik, J. M., Oh, S. Y., Schneewind, O., (2011) Nat. Rev. Microbiol., 9, p. 16
Kaprelyants, A. S., Mukamolova, G. V., Ruggiero, A., Makarov, V. A., Demina, G. R., Shleeva, M. O., Potapov, V. D., Shramko, P., (2011) Protein Pept. Lett., , not supplied
Shah, I. M., Laaberki, M. H., Popham, D. L., Dworkin, J., (2008) Cell, 135, p. 486
Lim, J. H., Kim, M. S., Kim, H. E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W. E., Oh, B. H., (2006) J. Biol. Chem., 281, p. 8286
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2011 Dec 28; 133(51): 20676-20679.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 9.907, 5-year impact factor: 9.766
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84555178075&partnerID=40&md5=1385a115e0ceea89e17d6e3defc8f053
Keywords: Arginine Residue, Bacillus Subtilis, Bacterial Spore, Cell Walls, Cellular Process, Extracellular Region, Growing Conditions, Molecular Signals, Muropeptides, Nmr Techniques, Peptidoglycans, Protein Mutagenesis, Structural Requirements, Bacteriology, Resuscitation, Walls (structural Partitions), Enzymes, Amino Acid Derivative, Bacterial Enzyme, Diaminopimelic Acid, Prkc Protein, Protein Serine Threonine Kinase, Unclassified Drug, Article, Bacterial Cell Wall, Bacterial Growth, Bacterial Survival, Binding Site, Carbohydrate Analysis, Carboxy Terminal Sequence, Cell Growth, Circular Dichroism, Controlled Study, Dormancy, Enzyme Binding, Extracellular Space, Germination, In Vitro Study, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Protein Domain, Protein Interaction, Protein Structure, Signal Transduction, Staphylococcus Aureus, Models, Mutation, Biomolecular, Protein Binding, Protein Conformation, Tertiary, Protein-Serine-Threonine Kinases, Substrate Specificity,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, Consiglio Nazionale Delle Ricerche (CNR), Via Mezzocannone 16, I-80134 Napoli, Italy
Department of Organic and Biological Chemistry, University of Naples Federico II, Via Cinthia 4, I-80126 Napoli, Italy
Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, United States
European Molecular Biology Laboratory, Hamburg Outstation, C/o DESY, Notkestrasse 85, 22607 Hamburg, Germany
References:
Hendrickx, A.P., Budzik, J.M., Oh, S.Y., Schneewind, O., (2011) Nat. Rev. Microbiol., 9, p. 16
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., (2009) J. Mol. Biol., 385, p. 153
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., (2010) Structure, 18, p. 1184
Kaprelyants, A.S., Mukamolova, G.V., Ruggiero, A., Makarov, V.A., Demina, G.R., Shleeva, M.O., Potapov, V.D., Shramko, P., (2011) Protein Pept. Lett., , not supplied
Shah, I.M., Laaberki, M.H., Popham, D.L., Dworkin, J., (2008) Cell, 135, p. 486
Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., Seror, S., (2002) Mol. Microbiol., 46, p. 571
Fiuza, M., Canova, M.J., Zanella-Cleon, I., Becchi, M., Cozzone, A.J., Mateos, L.M., Kremer, L., Molle, V., (2008) J. Biol. Chem., 283, p. 18099
Madec, E., Stensballe, A., Kjellstrom, S., Cladiere, L., Obuchowski, M., Jensen, O.N., Seror, S.J., (2003) J. Mol. Biol., 330, p. 459
Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I.B., Seror, S.J., (2009) Microbiology, 155, p. 932
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., (2011) Biochem. J., 435, p. 33
Meyer, B., Peters, T., (2003) Angew. Chem., Int. Ed., 42, p. 864
Angulo, J., Langpap, B., Blume, A., Biet, T., Meyer, B., Krishna, N.R.H., Peters, H., Peters, T., (2006) J. Am. Chem. Soc., 128, p. 13529
Roldos, V., Canada, F.J., Jimenez-Barbero, J., (2011) ChemBioChem, 12, p. 990
Mari, S., Serrano-Gomez, D., Canada, F.J., Corbi, A.L., Jimenez-Barbero, J., (2004) Angew. Chem., Int. Ed., 44, p. 296
Mayer, M., Meyer, B., (2001) J. Am. Chem. Soc., 123, p. 6108
Hu, X., Zhang, W., Carmichael, I., Serianni, A., (2010) J. Am. Chem. Soc., 132, p. 4641
Mieczkowski, C., Iavarone, A.T., Alber, T., (2008) EMBO J., 27, p. 3186
Debarbouille, M., Dramsi, S., Dussurget, O., Nahori, M.A., Vaganay, E., Jouvion, G., Cozzone, A., Duclos, B., (2009) J. Bacteriol., 191, p. 4070
Lim, J.H., Kim, M.S., Kim, H.E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W.E., Oh, B.H., (2006) J. Biol. Chem., 281, p. 8286
Mushtaq, M., Asong, J., Li, X., Cardot, J., Boons, G.-J., Husson, R.N., (2011) PLOS Pathog., 7, pp. e1002182
Schlessinger, J., Plotnikov, A.N., Ibrahimi, O.A., Eliseenkova, A.V., Yeh, B.K., Yayon, A., Linhardt, R.J., Mohammadi, M., (2000) Mol. Cell, 6, p. 743
Hendrickx, A. P., Budzik, J. M., Oh, S. Y., Schneewind, O., (2011) Nat. Rev. Microbiol., 9, p. 16
Kaprelyants, A. S., Mukamolova, G. V., Ruggiero, A., Makarov, V. A., Demina, G. R., Shleeva, M. O., Potapov, V. D., Shramko, P., (2011) Protein Pept. Lett., , not supplied
Shah, I. M., Laaberki, M. H., Popham, D. L., Dworkin, J., (2008) Cell, 135, p. 486
Lim, J. H., Kim, M. S., Kim, H. E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W. E., Oh, B. H., (2006) J. Biol. Chem., 281, p. 8286
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
Bacterial Ser/Thr kinases modulate a wide number of cellular processes. In Bacillus subtilis, the Ser/Thr kinase PrkC has been shown to induce germination of bacterial spores in response to DAP-type but not Lys-type cell wall muropeptides. Muropeptides are a clear molecular signal that growing conditions are promising, since they are produced during cell wall peptidoglycan remodeling associated with cell growth and division of neighboring bacteria. However, whether muropeptides are able to bind the protein physically and how the extracellular region is able to distinguish the two types of muropeptides remains unclear. Here we tackled the important question of how the extracellular region of PrkC (EC-PrkC) senses muropeptides. By coupling NMR techniques and protein mutagenesis, we exploited the structural requirements necessary for recognition and binding and proved that muropeptides physically bind to EC-PrkC through DAP-moiety-mediated interactions with an arginine residue, Arg500, belonging to the protein C-terminal PASTA domain. Notably, mutation of this arginine completely suppresses muropeptide binding. Our data provide the first molecular clues into the mechanism of sensing of muropeptides by PrkC. © 2011 American Chemical Society.
Bacterial Ser/Thr kinases modulate a wide number of cellular processes. In Bacillus subtilis, the Ser/Thr kinase PrkC has been shown to induce germination of bacterial spores in response to DAP-type but not Lys-type cell wall muropeptides. Muropeptides are a clear molecular signal that growing conditions are promising, since they are produced during cell wall peptidoglycan remodeling associated with cell growth and division of neighboring bacteria. However, whether muropeptides are able to bind the protein physically and how the extracellular region is able to distinguish the two types of muropeptides remains unclear. Here we tackled the important question of how the extracellular region of PrkC (EC-PrkC) senses muropeptides. By coupling NMR techniques and protein mutagenesis, we exploited the structural requirements necessary for recognition and binding and proved that muropeptides physically bind to EC-PrkC through DAP-moiety-mediated interactions with an arginine residue, Arg500, belonging to the protein C-terminal PASTA domain. Notably, mutation of this arginine completely suppresses muropeptide binding. Our data provide the first molecular clues into the mechanism of sensing of muropeptides by PrkC. © 2011 American Chemical Society.
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
| ▼ Cell wall recognition events for biosensors development |
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
Other filter: ([btitle,keywords] "Arginine Residue" OR ...
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)
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Graziano G, Merlino A
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Lin L-L, Chen Y-Y, Chi M-C, Merlino A
* Low resolution X-ray structure of γ-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion (696 views)
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Impact Factor: 4.882
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Kaprelyants AS, Mukamolova GV, Ruggiero A, Makarov VA, Demina GR, Shleeva MO, Potapov VD, Shramko PA
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Impact Factor: 1.994
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Contursi P, D'Ambrosio K, Pirone L, Pedone E, Aucelli T, She Q, De Simone G, Bartolucci S
* C68 from the Sulfolobus islandicus plasmid-virus pSSVx is a novel member of the AbrB-like transcription factor family (1016 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 157-166.
Impact Factor: 4.897
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 (600 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
D'Auria G, Esposito C, Falcigno L, Calvanese L, Iaccarino E, Ruggiero A, Pedone C, Pedone E, Berisio R
* Dynamical properties of cold shock protein A from Mycobacterium tuberculosis (321 views)
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Impact Factor: 2.595
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Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (248 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
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De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase (633 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
View Export to BibTeX Export to EndNote
* 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
Graziano G, Merlino A
* Molecular bases of protein halotolerance (408 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014 Apr; 1844(4): 850-858.
Impact Factor: 4.882
View Export to BibTeX Export to EndNote
Lin L-L, Chen Y-Y, Chi M-C, Merlino A
* Low resolution X-ray structure of γ-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion (696 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014; 1844(9): 1523-1529.
Impact Factor: 4.882
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
Contursi P, D'Ambrosio K, Pirone L, Pedone E, Aucelli T, She Q, De Simone G, Bartolucci S
* C68 from the Sulfolobus islandicus plasmid-virus pSSVx is a novel member of the AbrB-like transcription factor family (1016 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 157-166.
Impact Factor: 4.897
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 (600 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
D'Auria G, Esposito C, Falcigno L, Calvanese L, Iaccarino E, Ruggiero A, Pedone C, Pedone E, Berisio R
* Dynamical properties of cold shock protein A from Mycobacterium tuberculosis (321 views)
Biochem Biophys Res Commun (ISSN: 0006-291x, 1090-2104, 1090-2104electronic), 2010 Nov 26; 402(4): 693-698.
Impact Factor: 2.595
View Export to BibTeX Export to EndNote
Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (248 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
View Export to BibTeX Export to EndNote
De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase (633 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
View Export to BibTeX Export to EndNote
10 Records (10 excluding Abstracts).
Total impact factor: 41.989 (41.989 excluding Abstracts).
Total 5 year impact factor: 38.211 (38.211 excluding Abstracts).
Total impact factor: 41.989 (41.989 excluding Abstracts).
Total 5 year impact factor: 38.211 (38.211 excluding Abstracts).
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