Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/85154
Type: Artigo de periódico
Title: The C-terminal Region Of The Human P23 Chaperone Modulates Its Structure And Function
Author: Seraphim T.V.
Gava L.M.
Mokry D.Z.
Cagliari T.C.
Barbosa L.R.S.
Ramos C.H.I.
Borges J.C.
Abstract: The 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.
Editor: Academic Press Inc.
Rights: fechado
Identifier DOI: 10.1016/j.abb.2014.10.015
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84919363231&partnerID=40&md5=49673be94ae48274e593a5903464e488
Date Issue: 2015
Appears in Collections:Unicamp - Artigos e Outros Documentos

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