A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease

Michal R. Szymanski; Wangsheng Yu; Aleksandra M. Gmyrek; Mark A. White; Ian J. Molineux; J. Ching Lee; Y. Whitney Yin

doi:10.1038/ncomms14959

Nature Communications (May 2017)

A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease

Michal R. Szymanski,
Wangsheng Yu,
Aleksandra M. Gmyrek,
Mark A. White,
Ian J. Molineux,
J. Ching Lee,
Y. Whitney Yin

Affiliations

Michal R. Szymanski: Department of Pharmacology and Toxicology, University of Texas Medical Branch
Wangsheng Yu: Department of Pharmacology and Toxicology, University of Texas Medical Branch
Aleksandra M. Gmyrek: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch
Mark A. White: Sealy Center for Structural Biology, University of Texas Medical Branch
Ian J. Molineux: Department of Molecular Biosciences, University of Texas at Austin
J. Ching Lee: Sealy Center for Structural Biology, University of Texas Medical Branch
Y. Whitney Yin: Department of Pharmacology and Toxicology, University of Texas Medical Branch

DOI: https://doi.org/10.1038/ncomms14959
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 11

Abstract

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Human EXOG is crucial for mitochondrial DNA repair. Here the authors present the crystal structures of hEXOG in apo form and as DNA complex and suggest a `tape-measure' activity to generate optimal substrates for mitochondrial base excision repair.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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