Date of this Version
7-1-2016
Document Type
Article
Rights
default
Abstract
Protein-protein interactions are of special importance in cellular processes, including replication, transcription, recombination, and repair. Escherichia coli topoisomerase I (EcTOP1) is primarily involved in the relaxation of negative DNA supercoiling. E. coli RecA, the key protein for homologous recombination and SOS DNA-damage response, has been shown to stimulate the relaxation activity of EcTOP1. The evidence for their direct protein-protein interaction has not been previously established. We report here the direct physical interaction between E. coli RecA and topoisomerase I. We demonstrated the RecA-topoisomerase I interaction via pull-down assays, and surface plasmon resonance measurements. Molecular docking supports the observation that the interaction involves the topoisomerase I N-terminal domains that form the active site. Our results from pull-down assays showed that ATP, although not required, enhances the RecA-EcTOP1 interaction. We propose that E. coli RecA physically interacts with topoisomerase I to modulate the chromosomal DNA supercoiling.
DOI
10.1016/j.gene.2016.03.013
Identifier
27001450
Recommended Citation
Banda S, Tiwari PB, Darici Y, Tse-Dinh YC. Investigating direct interaction between Escherichia coli topoisomerase I and RecA. Gene. 2016;585(1):65-70. doi:10.1016/j.gene.2016.03.013
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Comments
Pubmed Accepted Manuscript
The publisher's final edited version of this article is available at Gene
Published in final edited form as: Gene. 2016 July 1; 585(1): 65–70. doi:10.1016/j.gene.2016.03.013.