Dataset Information

Identification of Bacillus subtilis YjoB-binding proteins using AP-MS

ABSTRACT: Bacillus subtilis YjoB has been an uncharacterized AAA+ ATPase which consists of a single ATPase domain and a unique N-terminal domain. To understand the molecular function of YjoB, we identified YjoB-binding proteins through proteomics approaches, and analyzed the relationship between YjoB and its binding proteins. YjoB was coeluted with catalase and iron-sulfur cluster proteins in affinity purification and enhanced the activity of a catalase by specifically preventing heat-induced aggregation of catalase.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Unusual Infection

SUBMITTER: Eunju Kwon

LAB HEAD: Dong Young Kim

PROVIDER: PXD032982 | Pride | 2022-10-12

REPOSITORIES: Pride

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Publications

Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.

Kwon Eunju E Dahal Pawan P Kim Dong Young DY

Proceedings of the National Academy of Sciences of the United States of America 20221003 41

AAA+ ATPases are ubiquitous proteins associated with most cellular processes, including DNA unwinding and protein unfolding. Their functional and structural properties are typically determined by domains and motifs added to the conserved ATPases domain. Currently, the molecular function and structure of many ATPases remain elusive. Here, we report the crystal structure and biochemical analyses of YjoB, a <i>Bacillus subtilis</i> AAA+ protein. The crystal structure revealed that the YjoB hexamer ...[more]

PMID: 36191235

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