Reverse-chaperoning activity of an AAA+ protein

Cheng Liu, Mary C. McKinney, Yi Hsing Chen, Tyler M. Earnest, Xinghua Shi, Li Jung Lin, Yoshizumi Ishino, Karin Dahmen, Isaac K.O. Cann, Taekjip Ha

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Speed and processivity of replicative DNA polymerases can be enhanced via coupling to a sliding clamp. Due to the closed ring shape of the clamp, a clamp loader protein, belonging to the AAA+ class of ATPases, needs to open the ring-shaped clamp before loading it to DNA. Here, we developed real-time fluorescence assays to study the clamp (PCNA) and the clamp loader (RFC) from the mesophilic archaeon Methanosarcina acetivorans. Unexpectedly, we discovered that RFC can assemble a PCNA ring from monomers in solution. A motion-based DNA polymerization assay showed that the PCNA assembled by RFC is functional. This PCNA assembly activity required the ATP-bound conformation of RFC. Our work demonstrates a reverse-chaperoning activity for an AAA+ protein that can act as a template for the assembly of another protein complex.

Original languageEnglish
Pages (from-to)1344-1352
Number of pages9
JournalBiophysical Journal
Issue number5
Publication statusPublished - Mar 2 2011

All Science Journal Classification (ASJC) codes

  • Biophysics


Dive into the research topics of 'Reverse-chaperoning activity of an AAA+ protein'. Together they form a unique fingerprint.

Cite this