The Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates

Doménech, R. ; Hernández-Cifre, J.G. ; Bacarizo, J. ; Díez-Peña, A.I. ; Martínez-Rodríguez, S. ; Cavasotto, C.N. ; de, la Torre ; Cámara-Artigás, A. ; Velázquez-Campoy, A. (Universidad de Zaragoza) ; Neira, J.L.

Resumen: The phosphotransferase system (PTS) is involved in the use of carbon sources in bacteria. Bacillus sphaericus, a bacterium with the ability to produce insecticidal proteins, is unable to use hexoses and pentoses as the sole carbon source, but it has ptsHI genes encoding the two general proteins of the PTS: enzyme I (EI) and the histidine phosphocarrier (HPr). In this work, we describe the biophysical and structural properties of HPr from B. sphaericus, HPrbs, and its affinity towards EI of other species to find out whether there is inter-species binding. Conversely to what happens to other members of the HPr family, HPrbs forms several self-associated species. The conformational stability of the protein is low, and it unfolds irreversibly during heating. The protein binds to the N-terminal domain of EI from Streptomyces coelicolor, EINsc, with a higher affinity than that of the natural partner of EINsc, HPrsc. Modelling of the complex between EINsc and HPrbs suggests that binding occurs similarly to that observed in other HPr species. We discuss the functional implications of the oligomeric states of HPrbs for the glycolytic activity of B. sphaericus, as well as a strategy to inhibit binding between HPrsc and EINsc.

Idioma: Inglés

DOI: 10.1371/journal.pone.0069307

Año: 2013

Publicado en: PLoS One 8, 7 (2013), e69307 [15 pp]
ISSN: 1932-6203

Factor impacto JCR: 3.534 (2013)

Categ. JCR: MULTIDISCIPLINARY SCIENCES rank: 8 / 56 = 0.143 (2013) - Q1 - T1

Financiación: info:eu-repo/grantAgreement/ES/DGA/PI044-09
Financiación: info:eu-repo/grantAgreement/ES/MICINN/BFU2008-02302-BMC
Financiación: info:eu-repo/grantAgreement/ES/MICINN/BFU2010-19451
Financiación: info:eu-repo/grantAgreement/ES/MICINN/BIO2009-13261-C02-01-02
Financiación: info:eu-repo/grantAgreement/ES/MICINN/P09-CVI-5063
Financiación: info:eu-repo/grantAgreement/ES/MINECO/CSD2008-00005
Financiación: info:eu-repo/grantAgreement/ES/MINECO/CTQ2011-24393

Tipo y forma: Article (Published version)

Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)