Differential roles of putative arginine fingers of AAA⁺ ATPases Rvb1 and Rvb2.

ABSTRACT: The evolutionarily conserved AAA⁺ ATPases Rvb1 and Rvb2 proteins form a heteromeric complex (Rvb1/2) required for assembly or remodeling of macromolecular complexes in essential cellular processes ranging from chromatin remodeling to ribosome biogenesis. Rvb1 and Rvb2 have a high degree of sequence and structural similarity, and both contain the classical features of ATPases of their clade, including an N-terminal AAA⁺ subdomain with the Walker A motif, an insertion domain that typically interacts with various binding partners, and a C-terminal AAA⁺ subdomain containing a Walker B motif, the Sensor I and II motifs, and an arginine finger. In this study, we find that despite the high degree of structural similarity, Rvb1 and Rvb2 have distinct active sites t

SUBMITTER: Warnock JL 

PROVIDER: S-EPMC11118528 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature