Shukla, Kaustubh and Thakur, Roshan Singh and Ganguli, Debayan and Rao, Desirazu Narasimha and Nagaraju, Ganesh (2017) Escherichia coli and Neisseria gonorrhoeae UvrD helicase unwinds G4 DNA structures. In: BIOCHEMICAL JOURNAL, 474 (21). pp. 3579-3597.
PDF
BIO_JOU_474_3579_2017.pdf - Published Version Restricted to Registered users only Download (8MB) | Request a copy |
Abstract
G-quadruplex (G4) secondary structures have been implicated in various biological processes, including gene expression, DNA replication and telomere maintenance. However, unresolved G4 structures impede replication progression which can lead to the generation of DNA double-strand breaks and genome instability. Helicases have been shown to resolve G4 structures to facilitate faithful duplication of the genome. Escherichia coli UvrD (EcUvrD) helicase plays a crucial role in nucleotide excision repair, mismatch repair and in the regulation of homologous recombination. Here, we demonstrate a novel role of E. coli and Neisseria gonorrhoeae UvrD in resolving G4 tetraplexes. EcUvrD and N. gonorrhoeae UvrD were proficient in unwinding previously characterized tetramolecular G4 structures. Notably, EcUvrD was equally efficient in resolving tetramolecular and bimolecular G4 DNA that were derived from the potential G4-forming sequences from the genome of E. coli. Interestingly, in addition to resolving intermolecular G4 structures, EcUvrD was robust in unwinding intramolecular G4 structures. These data for the first time provide evidence for the role of UvrD in the resolution of G4 structures, which has implications for the in vivo role of UvrD helicase in G4 DNA resolution and genome maintenance.
Item Type: | Journal Article |
---|---|
Publication: | BIOCHEMICAL JOURNAL |
Additional Information: | Copy right for this article belongs to the PORTLAND PRESS LTD, CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND |
Department/Centre: | Division of Biological Sciences > Biochemistry |
Date Deposited: | 11 Nov 2017 07:01 |
Last Modified: | 11 Nov 2017 07:01 |
URI: | http://eprints.iisc.ac.in/id/eprint/58188 |
Actions (login required)
View Item |