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dc.contributor.authorWang, Wenjian
dc.contributor.authorRasmussen, Tim
dc.contributor.authorHarding, Amanda J.
dc.contributor.authorBooth, Nuala A.
dc.contributor.authorBooth, Ian R.
dc.contributor.authorNaismith, James H.
dc.identifier.citationWang , W , Rasmussen , T , Harding , A J , Booth , N A , Booth , I R & Naismith , J H 2012 , ' Salt bridges regulate both dimer formation and monomeric flexibility in HdeB and may have a role in periplasmic chaperone function ' , Journal of Molecular Biology , vol. 415 , no. 3 , pp. 538-546 .
dc.identifier.otherPURE: 18094546
dc.identifier.otherPURE UUID: 8e441524-3e71-4bfb-9419-a0d75317ada5
dc.identifier.otherWOS: 000300028700008
dc.identifier.otherScopus: 84855860995
dc.description.abstractEscherichia coli and Gram-negative bacteria that live in the human gut must be able to tolerate rapid and large changes in environmental pH. Low pH irreversibly denatures and precipitates many bacterial proteins. While cytoplasmic proteins are well buffered against such swings, periplasmic proteins are not. Instead, it appears that some bacteria utilize chaperone proteins that stabilize periplasmic proteins, preventing their precipitation. Two highly expressed and related proteins, HdeA and HdeB, have been identified as acid-activated chaperones. The structure of HdeA is known and a mechanism for activation has been proposed. In this model, dimeric HdeA dissociates at low pH, and the exposed dimeric interface binds exposed hydrophobic surfaces of acid-denatured proteins, preventing their irreversible aggregation. We now report the structure and biophysical characterization of the HdeB protein. The monomer of HdeB shares a similar structure with HdeA, but its dimeric interface is different in composition and spatial location. We have used fluorescence to study the behavior of HdeB as pH is lowered, and like HdeA, it dissociates to monomers. We have identified one of the key intersubunit interactions that controls pH-induced monomerization. Our analysis identifies a structural interaction within the HdeB monomer that is disrupted as pH is lowered, leading to enhanced structural flexibility.
dc.relation.ispartofJournal of Molecular Biologyen
dc.rights© The Authors. This is an open access article, available from http://www.sciencedirect.comen
dc.subjectCrystal structureen
dc.subjectFluorescence measurementsen
dc.subjectHydrophobic residuesen
dc.subjectAcid responseen
dc.subjectpH titrationen
dc.subjectQH301 Biologyen
dc.titleSalt bridges regulate both dimer formation and monomeric flexibility in HdeB and may have a role in periplasmic chaperone functionen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

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