DNA translocation mechanism of an XPD family helicase
File(s)
Published version
OA Location
Author(s)
Cheng, Kaiying
Wigley, Dale B
Type
Journal Article
Abstract
The XPD family of helicases, that includes human disease-related FANCJ, DDX11 and RTEL1, are Superfamily 2 helicases that contain an iron-sulphur cluster domain, translocate on ssDNA in a 5'-3' direction and play important roles in genome stability. Consequently, mutations in several of these family members in eukaryotes cause human diseases. Family members in bacteria, such as the DinG helicase from Escherichia coli, are also involved in DNA repair. Here we present crystal structures of complexes of DinG bound to single-stranded DNA (ssDNA) in the presence and absence of an ATP analogue (ADP•BeF3), that suggest a mechanism for 5'-3' translocation along the ssDNA substrate. This proposed mechanism has implications for how those enzymes of the XPD family that recognise bulky DNA lesionsmight stall at these as the first step in initiating DNA repair. Biochemical data reveal roles for conserved residues that are mutated in human diseases.
Date Issued
2018-12-06
Date Acceptance
2018-12-05
Citation
eLife, 2018, 7
ISSN
2050-084X
Publisher
eLife Sciences Publications Ltd
Journal / Book Title
eLife
Volume
7
Copyright Statement
Copyright © Cheng and Wigley.
This article is distributed under
the terms of the Creative
Commons Attribution License,
which permits unrestricted use
and redistribution provided that
the original author and source are
credited.
This article is distributed under
the terms of the Creative
Commons Attribution License,
which permits unrestricted use
and redistribution provided that
the original author and source are
credited.
Sponsor
Medical Research Council (MRC)
Wellcome Trust
Identifier
https://www.ncbi.nlm.nih.gov/pubmed/30520735
PII: 42400
Grant Number
MR/N009258/1
202926/Z/16/Z
Subjects
E. coli
molecular biophysics
structural biology
Publication Status
Published
Coverage Spatial
England
Article Number
e42400