Artículos de revistas
The Histidine-Phosphocarrier protein of the Phosphoenolpyruvate: sugar Phosphotransferase system of Bacillus sphaericus self-associates
Fecha
2013-07Registro en:
Domenech, Rosa; Hernández Cifre, José G.; Bacarizo, Julio; Diez Peña, Ana I.; Martínez Rodríguez, Sergio; et al.; The Histidine-Phosphocarrier protein of the Phosphoenolpyruvate: sugar Phosphotransferase system of Bacillus sphaericus self-associates; Public Library of Science; Plos One; 8; 7; 7-2013; 1-15; e69307
1932-6203
CONICET Digital
CONICET
Autor
Domenech, Rosa
Hernández Cifre, José G.
Bacarizo, Julio
Diez Peña, Ana I.
Martínez Rodríguez, Sergio
Cavasotto, Claudio Norberto
García de la Torre, José
Cámara Artigás, Ana
Velázquez Campoy, Adrián
Neira, José 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.