An adenosine triphosphate-independent proteasome activator contributes to the virulence of Mycobacterium tuberculosis.

ABSTRACT: Mycobacterium tuberculosis encodes a proteasome that is highly similar to eukaryotic proteasomes and is required to cause lethal infections in animals. The only pathway known to target proteins for proteasomal degradation in bacteria is pupylation, which is functionally analogous to eukaryotic ubiquitylation. However, evidence suggests that the M. tuberculosis proteasome contributes to pupylation-independent pathways as well. To identify new proteasome cofactors that might contribute to such pathways, we isolated proteins that bound to proteasomes overproduced in M. tuberculosis and found a previously uncharacterized protein, Rv3780, which formed rings and capped M. tuberculosis proteasome core particles. Rv3780 enhanced peptide and protein degradation by proteasomes in an adenosine tripho

SUBMITTER: Jastrab JB 

PROVIDER: S-EPMC4394314 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature