Reverse-chaperoning activity of an AAA+ protein |
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| Authors: | Liu Cheng McKinney Mary C Chen Yi-Hsing Earnest Tyler M Shi Xinghua Lin Li-Jung Ishino Yoshizumi Dahmen Karin Cann Isaac K O Ha Taekjip |
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| Affiliation: | †Department of Physics and the Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Champaign, Illinois;‡Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Champaign, Illinois;§Department of Animal Sciences, University of Illinois at Urbana-Champaign, Champaign, Illinois;¶Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Champaign, Illinois;‖Department of Microbiology, University of Illinois at Urbana-Champaign, Champaign, Illinois;∗∗Howard Hughes Medical Institute, Urbana, Illinois;††Department of Genetic Resources, Faculty of Agriculture, Kyushu University, Fukuoka-shi, Japan |
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| Abstract: | ![]()
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. |
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