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Molecular mechanisms of xeroderma pigmentosum (XP) proteins

Published online by Cambridge University Press:  10 February 2016

Sandra C. Koch ,
Nina Simon ,
Charlotte Ebert  and
Thomas Carell
Sandra C. Koch
Affiliation:
Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians Universität München, Butenandtstr. 5-13, 81377 Munich, Germany
Nina Simon
Affiliation:
Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians Universität München, Butenandtstr. 5-13, 81377 Munich, Germany
Charlotte Ebert
Affiliation:
Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians Universität München, Butenandtstr. 5-13, 81377 Munich, Germany
Thomas Carell*
Affiliation:
Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians Universität München, Butenandtstr. 5-13, 81377 Munich, Germany
*
*Authors for correspondence: Thomas Carell, Center for Integrated Protein Science at the Department of Chemistry, Ludwig-Maximilians Universität München, Butenandtstr, 5-13, 81377 Munich, Germany. Tel.: +49 (0)89 2180 77755 Email: thomas.carell@cup.uni-muenchen.de
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Abstract

Nucleotide excision repair (NER) is a highly versatile and efficient DNA repair process, which is responsible for the removal of a large number of structurally diverse DNA lesions. Its extreme broad substrate specificity ranges from DNA damages formed upon exposure to ultraviolet radiation to numerous bulky DNA adducts induced by mutagenic environmental chemicals and cytotoxic drugs used in chemotherapy. Defective NER leads to serious diseases, such as xeroderma pigmentosum (XP). Eight XP complementation groups are known of which seven (XPA–XPG) are caused by mutations in genes involved in the NER process. The eighth gene, XPV, codes for the DNA polymerase ɳ, which replicates through DNA lesions in a process called translesion synthesis (TLS). Over the past decade, detailed structural information of these DNA repair proteins involved in eukaryotic NER and TLS have emerged. These structures allow us now to understand the molecular mechanism of the NER and TLS processes in quite some detail and we have begun to understand the broad substrate specificity of NER. In this review, we aim to highlight recent advances in the process of damage recognition and repair as well as damage tolerance by the XP proteins.

Keywords

NERxeroderma pigmentosumcrystal structuresDNA repair
Type
Review
Information
Quarterly Reviews of Biophysics , Volume 49 , 2016 , e5
Copyright
Copyright © Cambridge University Press 2016 

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