RecA stimulates AlkB-mediated direct repair of DNA adducts

Gururaj, S and Mohan, M and Nigam, R and Kodipelli, N and Roy, Anindya (2016) RecA stimulates AlkB-mediated direct repair of DNA adducts. Nucleic Acids Research. pp. 1-10. ISSN 0305-1048

Text (Open access)
Nucl. Acids Res.-2016-Shivange-nar_gkw611.pdf - Published Version
Available under License Creative Commons Attribution.

Download (1MB) | Preview


The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein. The interaction between AlkB and RecA was validated by yeast two-hybrid assay; size-exclusion chromatography and standard pull down experiment and was shown to be direct and mediated by the N-terminal domain of RecA. RecA binding results AlkB–RecA heterodimer formation and RecA–AlkB repairs alkylated DNA with higher efficiency than AlkB alone.

[error in script]
IITH Creators:
IITH CreatorsORCiD
Roy, Anindya
Item Type: Article
Additional Information: We thank Dr Luke A. Selth, Dame Roma Mitchell Cancer Research Laboratories and Adelaide Prostate Cancer Re- search Centre, The University of Adelaide, SA, Australia for editing the manuscript. We thank Dr N. Ganesh (Indian Institute of Science, Bangalore) and Dr K. Gopinath (Uni- versity of Hyderabad, Hyderabad) for reagents and techni- cal help.
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Team Library
Date Deposited: 12 Jul 2016 05:42
Last Modified: 05 Dec 2017 05:00
Publisher URL:
OA policy:
Related URLs:

Actions (login required)

View Item View Item
Statistics for RAIITH ePrint 2527 Statistics for this ePrint Item