Structural insights into the Pseudomonas aeruginosa ClpP1•ClpP2 heterocomplex and its interactions with the AAA+ ClpX unfoldase.

ABSTRACT: ClpXP and other AAA+ proteases play central roles in bacterial proteostasis by degrading misfolded and regulatory proteins. In Pseudomonas aeruginosa, ClpXP consists of the ClpX unfoldase and ClpP peptidase, which influence critical adaptive processes contributing to stress resistance. P. aeruginosa ^PaClpP1 and ^PaClpP2 paralogs assemble into homomeric (^PaClpP1•ClpP1) and heteromeric (^PaClpP1•ClpP2) complexes. ^PaClpP2 is only active in the ^PaClpP1•ClpP2 heterocomplex. Here, we present a cryo-EM structure of ^PaClpX•ClpP1•ClpP2, revealing how ^PaClpX binds ^PaClpP1, which in turn interacts with ^PaClpP2. Comparison of the active heterocomplex with an inactive ^PaClpP2 crystal s

SUBMITTER: Ghanbarpour A 

PROVIDER: S-EPMC12451819 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature