Chemical basis of peptidoglycandiscrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Chemical basis of peptidoglycandiscrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1021/ja208080r (literal)

Alternative label

• Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, Dworkin J, Petoukhov M, Molinaro A, Berisio R, Silipo A. (2011)
  Chemical basis of peptidoglycandiscrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
  in Journal of the American Chemical Society (Online)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, Dworkin J, Petoukhov M, Molinaro A, Berisio R, Silipo A. (literal)

Pagina inizio

• 20676 (literal)

Pagina fine

• 20679 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 133 (literal)

Rivista

• Journal of the American Chemical Society (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 4 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 51 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Institute of Biostructures and Bioimaging, Consiglio Nazionale delle Ricerche (CNR), Napoli, Italy. (literal)

Titolo

• Chemical basis of peptidoglycandiscrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy (literal)

Abstract

• 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. (literal)

Prodotto di

• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• ANTONIO MOLINARO (Persona)
• ALESSIA RUGGIERO (Unità di personale interno)
• DANIELA MARASCO (Unità di personale esterno)
• RITA BERISIO (Unità di personale interno)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)

Autore CNR di

• RITA BERISIO (Unità di personale interno)
• DANIELA MARASCO (Unità di personale esterno)
• ANTONIO MOLINARO (Persona)
• ALESSIA RUGGIERO (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of the American Chemical Society (Rivista)