Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.

ABSTRACT: Aha1 is the only co-chaperone known to strongly stimulate the ATPase activity of Hsp90. Meanwhile, besides the well-studied co-chaperone function, human Aha1 has also been demonstrated to exhibit chaperoning activity against stress-denatured proteins. To provide structural insights for a better understanding of Aha1's co-chaperone and chaperone-like activities, nuclear magnetic resonance (NMR) techniques were used to reveal the unique structure and internal dynamics features of full-length human Aha1. We then found that, in solution, both the two domains of Aha1 presented distinctive thermal stabilities and dynamics behaviors defined by their primary sequences and three-dimensional structures. The low thermal stability (melting temperature of Aha1^28-162: 54.45 °C) and the intern

SUBMITTER: Hu H 

PROVIDER: S-EPMC8037086 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature