The C-terminal Region Of The Human P23 Chaperone Modulates Its Structure And Function.
Contribuinte(s) |
UNIVERSIDADE DE ESTADUAL DE CAMPINAS |
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Data(s) |
01/01/2015
27/11/2015
27/11/2015
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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 |