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| Title | The C-terminal region of the human p23 chaperone modulates its structure and function. |
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| Journal, issue, pages | Arch Biochem Biophys, Vol. 565, Page 57-67, Year 2015 |
| Publish date | Jan 1, 2015 |
 Authors | Thiago V Seraphim / Lisandra M Gava / David Z Mokry / Thiago C Cagliari / Leandro R S Barbosa / Carlos H I Ramos / Júlio C Borges /  |
| PubMed 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, ...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. |
 External links | Arch Biochem Biophys / PubMed:25447839 |
| Methods | SAS (X-ray synchrotron) |
| Structure data |  SASDBH6: Full-length human p23 (1-160) (Prostaglandin E synthase 3, PTGES, Sba1, p23)  SASDBJ6: Truncated construct of human p23 (1-142) (Prostaglandin E synthase 3 (1-142), PTGES, Sba1, p23)  SASDBK6: Truncated construct of human p23 (1-131) (Prostaglandin E synthase 3 (1-131), PTGES, Sba1, p23)  SASDBL6: Truncated construct of human p23 (1-117) (Prostaglandin E synthase 3 (1-117), PTGES, Sba1, p23) |
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Homo sapiens (human)