The histidine-phosphocarrier protein of the phosphoenolpyruvate: sugar phosphotransferase system of Bacillus sphaericus self-associates
Autor: | Claudio N. Cavasotto, Ana Isabel Díez-Peña, José García de la Torre, Julio Bacarizo, Ana Cámara-Artigas, José G. Hernández-Cifre, Sergio Martínez-Rodríguez, Adrián Velázquez-Campoy, José L. Neira, Rosa Doménech |
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Přispěvatelé: | Ministerio de Ciencia e Innovación (España), European Commission, Diputación General de Aragón, Junta de Andalucía, Agencia Nacional de Promoción Científica y Tecnológica (Argentina), Instituto de Biocomputación y Física de Sistemas Complejos (España) |
Rok vydání: | 2013 |
Předmět: |
Models
Molecular Proteomics BACILUS SPHAERICUS Protein Denaturation Protein Folding Hot Temperature lcsh:Medicine Bacillus Plasma protein binding Bacillus sphaericus Biochemistry Protein Structure Secondary purl.org/becyt/ford/1 [https] Protein structure ENZYME I Macromolecular Structure Analysis Phosphorylation Biomacromolecule-Ligand Interactions lcsh:Science Multidisciplinary biology Physics Streptomyces coelicolor PEP group translocation Bioquímica y Biología Molecular Hydrogen-Ion Concentration PROTEIN-PROTEIN INTERACTION Thermodynamics Phosphoenolpyruvate carboxykinase CIENCIAS NATURALES Y EXACTAS Protein Binding Research Article Protein Structure Biophysics Phosphocarrier protein macromolecular substances Calorimetry Protein Chemistry Ciencias Biológicas Bacterial Proteins Histidine purl.org/becyt/ford/1.6 [https] Phosphoenolpyruvate Sugar Phosphotransferase System Protein Interactions Biology lcsh:R fungi Proteins Computational Biology biology.organism_classification carbohydrates (lipids) Spectrometry Fluorescence HISTIDINE-PHOSPHOCARRIER PROTEIN biology.protein Hydrodynamics bacteria lcsh:Q Peptides |
Zdroj: | PLoS ONE Digital.CSIC: Repositorio Institucional del CSIC Consejo Superior de Investigaciones Científicas (CSIC) CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET PLoS ONE, Vol 8, Iss 7, p e69307 (2013) Digital.CSIC. Repositorio Institucional del CSIC instname |
ISSN: | 1932-6203 |
Popis: | 15 pags, 7 figs, 1 tab 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. © 2013 Doménech et al. This work was supported by the Spanish Ministerio de Ciencia e Innovación (MCINN) (CTQ2011-24393, and CSD2008-00005 to JLN; BIO2009-13261-C02- 01/02 and P09-CVI-5063, with Fondo Social Europeo (ESF) to ACA; and BFU2010-19451 to AVC), Diputación General de Aragón (PI044/09 to AVC), intramural BIFI 2011 projects (to AVC and JLN), Junta de Andalucía (BIO-328 to ACA), and by grants from the Agencia Nacional de Promoción Científica y Tecnológica Argentina (ANPCyT; PICT-2011-2778) (to CNC). SMR was supported by the CSD2008-00005. The stays of RD in the laboratory of AVC were supported by the Spanish Ministerio de Ciencia e Innovación (BFU2008-02302-BMC). |
Databáze: | OpenAIRE |
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