The HRDC domain oppositely modulates the unwinding activity of E. coli RecQ helicase on duplex DNA and G-quadruplex.
DNA
/ metabolism
DNA Repair
Escherichia coli
/ enzymology
Fluorescence Resonance Energy Transfer
G-Quadruplexes
Humans
Mutagenesis, Site-Directed
Nucleic Acid Conformation
Protein Binding
Protein Domains
Protein Structure, Tertiary
RecQ Helicases
/ chemistry
Recombinant Proteins
/ biosynthesis
Substrate Specificity
DNA repair
E. coli
G-quadruplex
RecQ
helicase
single-molecule
unwinding
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
18 12 2020
18 12 2020
Historique:
received:
10
08
2020
revised:
09
10
2020
entrez:
17
1
2021
pubmed:
18
1
2021
medline:
2
4
2021
Statut:
ppublish
Résumé
RecQ family helicases are highly conserved from bacteria to humans and have essential roles in maintaining genome stability. Mutations in three human RecQ helicases cause severe diseases with the main features of premature aging and cancer predisposition. Most RecQ helicases shared a conserved domain arrangement which comprises a helicase core, an RecQ C-terminal domain, and an auxiliary element helicase and RNaseD C-terminal (HRDC) domain, the functions of which are poorly understood. In this study, we systematically characterized the roles of the HRDC domain in E. coli RecQ in various DNA transactions by single-molecule FRET. We found that RecQ repetitively unwinds the 3'-partial duplex and fork DNA with a moderate processivity and periodically patrols on the ssDNA in the 5'-partial duplex by translocation. The HRDC domain significantly suppresses RecQ activities in the above transactions. In sharp contrast, the HRDC domain is essential for the deep and long-time unfolding of the G4 DNA structure by RecQ. Based on the observations that the HRDC domain dynamically switches between RecA core- and ssDNA-binding modes after RecQ association with DNA, we proposed a model to explain the modulation mechanism of the HRDC domain. Our findings not only provide new insights into the activities of RecQ on different substrates but also highlight the novel functions of the HRDC domain in DNA metabolisms.
Identifiants
pubmed: 33454004
pii: S0021-9258(17)50646-8
doi: 10.1074/jbc.RA120.015492
pmc: PMC7762929
pii:
doi:
Substances chimiques
Recombinant Proteins
0
DNA
9007-49-2
RecQ protein, E coli
EC 3.6.1.-
RecQ Helicases
EC 3.6.4.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
17646-17658Informations de copyright
Copyright © 2020 © 2020 Teng et al. Published by Elsevier Inc. All rights reserved.
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