Journal Article

The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility

Kyle T Powers, Adrian H Elcock and M Todd Washington

in Nucleic Acids Research

Volume 46, issue 4, pages 2107-2120
Published in print February 2018 | ISSN: 0305-1048
Published online January 2018 | e-ISSN: 1362-4962 | DOI: http://dx.doi.org/10.1093/nar/gky031
The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility

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  • Enzymology
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Abstract

Eukaryotic DNA polymerase η catalyzes translesion synthesis of thymine dimers and 8-oxoguanines. It is comprised of a polymerase domain and a C-terminal region, both of which are required for its biological function. The C-terminal region mediates interactions with proliferating cell nuclear antigen (PCNA) and other translesion synthesis proteins such as Rev1. This region contains a ubiquitin-binding/zinc-binding (UBZ) motif and a PCNA-interacting protein (PIP) motif. Currently little structural information is available for this region of polymerase η. Using a combination of approaches—including genetic complementation assays, X-ray crystallography, Langevin dynamics simulations, and small-angle X-ray scattering—we show that the C-terminal region is partially unstructured and has high conformational flexibility. This implies that the C-terminal region acts as a flexible tether linking the polymerase domain to PCNA thereby increasing its local concentration. Such tethering would facilitate the sampling of translesion synthesis polymerases to ensure that the most appropriate one is selected to bypass the lesion.

Journal Article.  9555 words.  Illustrated.

Subjects: Enzymology ; Molecular Biology and Genetics ; Bioinformatics and Computational Biology

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