Cooperative assembly of p97 complexes involved in replication termination.

ABSTRACT: The p97 ATPase extracts polyubiquitylated proteins from diverse cellular structures in preparation for destruction by the proteasome. p97 functions with Ufd1-Npl4 and a variety of UBA-UBX co-factors, but how p97 complexes assemble on ubiquitylated substrates is unclear. To address this, we investigated how p97 disassembles the CMG helicase after it is ubiquitylated during replication termination. We show that p97^Ufd1-Npl4 recruitment to CMG requires the UBA-UBX protein Ubxn7, and conversely, stable Ubxn7 binding to CMG requires p97^Ufd1-Npl4. This cooperative assembly involves interactions between Ubxn7, p97, Ufd1-Npl4, and ubiquitin. Another p97 co-factor, Faf1, partially compensates for the loss of Ubxn7. Surprisingly, p97^{Ufd1-Npl4-Ubxn7} and p97^Ufd1-N

SUBMITTER: Kochenova OV 

PROVIDER: S-EPMC9633789 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature