Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
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Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (590 views)

Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, Dworkin J, Petoukhov M, Molinaro A, Berisio R, Silipo A

J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2011 Dec 28; 133(51): 20676-20679.

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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:
Not available.
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.
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

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Kaprelyants AS, Mukamolova GV, Ruggiero A, Makarov VA, Demina GR, Shleeva MO, Potapov VD, Shramko PA
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Contursi P, D'Ambrosio K, Pirone L, Pedone E, Aucelli T, She Q, De Simone G, Bartolucci S
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Impact Factor: 4.897
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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 (1321 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2011 Apr 1; 435(1): 33-41.
Impact Factor: 4.897
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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 (732 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 (594 views)
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Impact Factor: 1.47
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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 (847 views)
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De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C
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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).

Last modified by Marco Comerci on Sunday 12 July 2020, 13:14:58
590 views. Last view on Thursday 24 April 2025, 0:20:01