Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease.

ABSTRACT: Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane-bound ATP-dependent processive metalloprotease FtsH and cleaves MgtE, the major high-affinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn²⁺ /Zn²⁺ toxicity. The N-terminal cytosolic domain of YqgP binds Mn²⁺ and Zn²⁺ ions and facilitates MgtE cleavage. Independently of it

SUBMITTER: Began J 

PROVIDER: S-EPMC7231995 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature