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J Bacteriol. 1994 March; 176(5): 1405-1412

research-article

The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization.

Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.

ABSTRACT

We have cloned, expressed, and purified the RecA analog from the thermophilic eubacterium Thermus aquaticus YT-1. Analysis of the deduced amino acid sequence indicates that the T. aquaticus RecA is structurally similar to the Escherichia coli RecA and suggests that RecA-like function has been conserved in thermophilic organisms. Preliminary biochemical analysis indicates that the protein has an ATP-dependent single-stranded DNA binding activity and can pair and carry out strand exchange to form a heteroduplex DNA under reaction conditions previously described for E. coli RecA, but at 55 to 65 degrees C. Further characterization of a thermophilically derived RecA protein should yield important information concerning DNA-protein interactions at high temperatures. In addition, a thermostable RecA protein may have some general applicability in stabilizing DNA-protein interactions in reactions which occur at high temperatures by increasing the specificity (stringency) of annealing reactions.

This article has been cited by other articles:

• Shigemori, Y., Mikawa, T., Shibata, T., Oishi, M. (2005). Multiplex PCR: use of heat-stable Thermus thermophilus RecA protein to minimize non-specific PCR products. Nucleic Acids Res 33: e126-e126 [Abstract] [Full Text]  
• Biswas, I., Hsieh, P. (1996). Identification and Characterization of a Thermostable MutS Homolog from Thermus aquaticus. J. Biol. Chem. 271: 5040-5048 [Abstract] [Full Text]