New insights into structural and functional relationships between LonA proteases and ClpB chaperones.

ABSTRACT: LonA proteases and ClpB chaperones are key components of the protein quality control system in bacterial cells. LonA proteases form a unique family of ATPases associated with diverse cellular activities (AAA⁺ ) proteins due to the presence of an unusual N-terminal region comprised of two domains: a β-structured N domain and an α-helical domain, including the coiled-coil fragment, which is referred to as HI(CC). The arrangement of helices in the HI(CC) domain is reminiscent of the structure of the H1 domain of the first AAA⁺ module of ClpB chaperones. It has been hypothesized that LonA proteases with a single AAA⁺ module may also contain a part of another AAA⁺ module, the full version of which is present in ClpB. Here, we established and tested th

SUBMITTER: Rotanova TV 

PROVIDER: S-EPMC6722904 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature