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):

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