000063310 001__ 63310
000063310 005__ 20210526094556.0
000063310 0247_ $$2doi$$a10.1371/journal.pone.0067961
000063310 0248_ $$2sideral$$a91111
000063310 037__ $$aART-2013-91111
000063310 041__ $$aeng
000063310 100__ $$aAprile F.A.
000063310 245__ $$aHsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain
000063310 260__ $$c2013
000063310 5060_ $$aAccess copy available to the general public$$fUnrestricted
000063310 5203_ $$aOligomerization in the heat shock protein (Hsp) 70 family has been extensively documented both in vitro and in vivo, although the mechanism, the identity of the specific protein regions involved and the physiological relevance of this process are still unclear. We have studied the oligomeric properties of a series of human Hsp70 variants by means of nanoelectrospray ionization mass spectrometry, optical spectroscopy and quantitative size exclusion chromatography. Our results show that Hsp70 oligomerization takes place through a specific interaction between the interdomain linker of one molecule and the substrate-binding domain of a different molecule, generating dimers and higher-order oligomers. We have found that substrate binding shifts the oligomerization equilibrium towards the accumulation of functional monomeric protein, probably by sequestering the helical lid sub-domain needed to stabilize the chaperone: substrate complex. Taken together, these findings suggest a possible role of chaperone oligomerization as a mechanism for regulating the availability of the active monomeric form of the chaperone and for the control of substrate binding and release.
000063310 536__ $$9info:eu-repo/grantAgreement/EC/FP7//EU//HFSP
000063310 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000063310 590__ $$a3.534$$b2013
000063310 591__ $$aMULTIDISCIPLINARY SCIENCES$$b8 / 56 = 0.143$$c2013$$dQ1$$eT1
000063310 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000063310 700__ $$aDhulesia A.
000063310 700__ $$aStengel F.
000063310 700__ $$aRoodveldt C.
000063310 700__ $$aBenesch J.L.
000063310 700__ $$aTortora P.
000063310 700__ $$aRobinson C.V.
000063310 700__ $$aSalvatella X.
000063310 700__ $$aDobson C.M.
000063310 700__ $$0(orcid)0000-0002-9138-6687$$aCremades Casasin, Nunilo
000063310 773__ $$g8, 6 (2013), e67961 [17 pp]$$pPLoS One$$tPloS one$$x1932-6203
000063310 8564_ $$s881360$$uhttps://zaguan.unizar.es/record/63310/files/texto_completo.pdf$$yVersión publicada
000063310 8564_ $$s138484$$uhttps://zaguan.unizar.es/record/63310/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000063310 909CO $$ooai:zaguan.unizar.es:63310$$particulos$$pdriver
000063310 951__ $$a2021-05-26-09:31:13
000063310 980__ $$aARTICLE