Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/202299
Type: Artigo de periódico
Title: The C-terminal Region Of The Human P23 Chaperone Modulates Its Structure And Function.
Author: Seraphim, Thiago V
Gava, Lisandra M
Mokry, David Z
Cagliari, Thiago C
Barbosa, Leandro R S
Ramos, Carlos H I
Borges, Júlio 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.
Subject: Hot Temperature
Humans
Molecular Chaperones
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
Structure-activity Relationship
Hsp90
Molecular Chaperone
Sba1
P19
P23
Rights: fechado
Identifier DOI: 10.1016/j.abb.2014.10.015
Address: http://www.ncbi.nlm.nih.gov/pubmed/25447839
Date Issue: 2015
Appears in Collections:Unicamp - Artigos e Outros Documentos

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