000063304 001__ 63304
000063304 005__ 20171129112117.0
000063304 0247_ $$2doi$$a10.1371/journal.pone.0069307
000063304 0248_ $$2sideral$$a82599
000063304 037__ $$aART-2013-82599
000063304 041__ $$aeng
000063304 100__ $$aDoménech, R.
000063304 245__ $$aThe Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates
000063304 260__ $$c2013
000063304 5060_ $$aAccess copy available to the general public$$fUnrestricted
000063304 5203_ $$aThe 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.
000063304 536__ $$9info:eu-repo/grantAgreement/ES/DGA/PI044-09$$9info:eu-repo/grantAgreement/ES/MICINN/BFU2008-02302-BMC$$9info:eu-repo/grantAgreement/ES/MICINN/BFU2010-19451$$9info:eu-repo/grantAgreement/ES/MICINN/BIO2009-13261-C02-01-02$$9info:eu-repo/grantAgreement/ES/MICINN/P09-CVI-5063$$9info:eu-repo/grantAgreement/ES/MINECO/CSD2008-00005$$9info:eu-repo/grantAgreement/ES/MINECO/CTQ2011-24393
000063304 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000063304 590__ $$a3.534$$b2013
000063304 591__ $$aMULTIDISCIPLINARY SCIENCES$$b8 / 56 = 0.143$$c2013$$dQ1$$eT1
000063304 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000063304 700__ $$aHernández-Cifre, J.G.
000063304 700__ $$aBacarizo, J.
000063304 700__ $$aDíez-Peña, A.I.
000063304 700__ $$aMartínez-Rodríguez, S.
000063304 700__ $$aCavasotto, C.N.
000063304 700__ $$ade, la Torre
000063304 700__ $$aCámara-Artigás, A.
000063304 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, A.$$uUniversidad de Zaragoza
000063304 700__ $$aNeira, J.L.
000063304 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDepartamento de Bioquímica y Biología Molecular y Celular$$cBioquímica y Biología Molecular
000063304 773__ $$g8, 7 (2013), e69307 [15 pp]$$pPLoS One$$tPLoS One$$x1932-6203
000063304 8564_ $$s307318$$uhttps://zaguan.unizar.es/record/63304/files/texto_completo.pdf$$yVersión publicada
000063304 8564_ $$s128424$$uhttps://zaguan.unizar.es/record/63304/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000063304 909CO $$ooai:zaguan.unizar.es:63304$$particulos$$pdriver
000063304 951__ $$a2017-11-28-12:46:14
000063304 980__ $$aARTICLE