Mapping the structural heterogeneity of Pup ligase PafA using H/D exchange mass spectrometry.

ABSTRACT: The Pup-proteasome system (PPS) is a unique bacterial proteolytic pathway found in some bacterial species, including in Mycobacterium tuberculosis, that plays a vital role in maintaining proteome integrity and survival during infection. Pupylation is the process of tagging substrates with Pup for degradation and is catalyzed by PafA, the sole Pup ligase in bacteria. However, how PafA interacts with diverse targets and its oligomeric state remains poorly understood. Although X-ray crystal structures have characterized PafA as a domain-swapped dimer, it is widely regarded as functionally active in its monomeric form. It remains to be established whether PafA dimerizes in solution, and how dimerization influences its function. In this study, we employed hydrogen-deuterium exchange mass spectr

SUBMITTER: Plourde A 

PROVIDER: S-EPMC12053664 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature