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 journalArticle


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 (US)
Pages (from-to)1344-1352
Number of pages9
JournalBiophysical journal
Issue number5
StatePublished - Mar 2 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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  • Cite this

    Liu, C., McKinney, M. C., Chen, Y. H., Earnest, T. M., Shi, X., Lin, L. J., Ishino, Y., Dahmen, K., Cann, I. K. O., & Ha, T. (2011). Reverse-chaperoning activity of an AAA+ protein. Biophysical journal, 100(5), 1344-1352.