The C-terminal Region Of The Human P23 Chaperone Modulates Its Structure And Function.

dc.creatorSeraphim, Thiago V
dc.creatorGava, Lisandra M
dc.creatorMokry, David Z
dc.creatorCagliari, Thiago C
dc.creatorBarbosa, Leandro R S
dc.creatorRamos, Carlos H I
dc.creatorBorges, Júlio C
dc.date2015-Jan
dc.date2015-11-27T13:46:42Z
dc.date2015-11-27T13:46:42Z
dc.date.accessioned2018-03-29T01:24:12Z
dc.date.available2018-03-29T01:24:12Z
dc.identifierArchives Of Biochemistry And Biophysics. v. 565, p. 57-67, 2015-Jan.
dc.identifier1096-0384
dc.identifier10.1016/j.abb.2014.10.015
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/25447839
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/202299
dc.identifier25447839
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1302532
dc.descriptionThe p23 protein is a chaperone widely involved in protein homeostasis, well known as an Hsp90 co-chaperone since it also controls the Hsp90 chaperone cycle. Human p23 includes a β-sheet domain, responsible for interacting with Hsp90; and a charged C-terminal region whose function is not clear, but seems to be natively unfolded. p23 can undergo caspase-dependent proteolytic cleavage to form p19 (p231-142), which is involved in apoptosis, while p23 has anti-apoptotic activity. To better elucidate the function of the human p23 C-terminal region, we studied comparatively the full-length human p23 and three C-terminal truncation mutants: p23₁₋₁₁₇; p23₁₋₁₃₁ and p23₁₋₁₄₂. Our data indicate that p23 and p19 have distinct characteristics, whereas the other two truncations behave similarly, with some differences to p23 and p19. We found that part of the C-terminal region can fold in an α-helix conformation and slightly contributes to p23 thermal-stability, suggesting that the C-terminal interacts with the β-sheet domain. As a whole, our results suggest that the C-terminal region of p23 is critical for its structure-function relationship. A mechanism where the human p23 C-terminal region behaves as an activation/inhibition module for different p23 activities is proposed.
dc.description565
dc.description57-67
dc.languageeng
dc.relationArchives Of Biochemistry And Biophysics
dc.relationArch. Biochem. Biophys.
dc.rightsfechado
dc.rightsCopyright © 2014 Elsevier Inc. All rights reserved.
dc.sourcePubMed
dc.subjectHot Temperature
dc.subjectHumans
dc.subjectMolecular Chaperones
dc.subjectProtein Stability
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.subjectStructure-activity Relationship
dc.subjectHsp90
dc.subjectMolecular Chaperone
dc.subjectSba1
dc.subjectP19
dc.subjectP23
dc.titleThe C-terminal Region Of The Human P23 Chaperone Modulates Its Structure And Function.
dc.typeArtículos de revistas


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