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


Autoria(s): Seraphim, Thiago V; Gava, Lisandra M; Mokry, David Z; Cagliari, Thiago C; Barbosa, Leandro R S; Ramos, Carlos H I; Borges, Júlio C
Contribuinte(s)

UNIVERSIDADE DE ESTADUAL DE CAMPINAS

Data(s)

01/01/2015

27/11/2015

27/11/2015

Resumo

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.

565

57-67

Identificador

Archives Of Biochemistry And Biophysics. v. 565, p. 57-67, 2015-Jan.

1096-0384

10.1016/j.abb.2014.10.015

http://www.ncbi.nlm.nih.gov/pubmed/25447839

http://repositorio.unicamp.br/jspui/handle/REPOSIP/202299

25447839

Idioma(s)

eng

Relação

Archives Of Biochemistry And Biophysics

Arch. Biochem. Biophys.

Direitos

fechado

Copyright © 2014 Elsevier Inc. All rights reserved.

Fonte

PubMed

Palavras-Chave #Hot Temperature #Humans #Molecular Chaperones #Protein Stability #Protein Structure, Secondary #Protein Structure, Tertiary #Structure-activity Relationship #Hsp90 #Molecular Chaperone #Sba1 #P19 #P23
Tipo

Artigo de periódico