PMID:9857048
| Citation |
Viswanathan, M, Dower, KW and Lovett, ST (1998) Identification of a potent DNase activity associated with RNase T of Escherichia coli. J. Biol. Chem. 273:35126-31 |
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| Abstract |
RNase T was first identified as an enzyme responsible for end turnover of tRNA in Escherichia coli. Its activity, specific for tRNA-C-C-A, catalyzes the release of tRNA-C-C and AMP. RNase T, along with several other RNases, plays a role in maturation of several other RNA species by a similar limited nuclease activity. In previous work, we identified the gene for RNase T, rnt, as a high copy suppressor of the UV sensitivity conferred by deficiency in three single-strand DNA-specific exonucleases, RecJ, exonuclease I, and exonuclease VII. This suggested that RNase T may process DNA substrates as well. In this work, we show that purified RNase T possesses a potent 3' to 5' single-strand DNA-specific exonucleolytic activity. Its Km for single-strand DNA substrates is many orders of magnitude lower than that for tRNA, suggesting that single-strand DNA may be a natural biological substrate for RNase T. We suggest that the DNase activity of RNase T may play a role in end trimming reactions during DNA recombination and/or DNA repair. |
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| Keywords |
DNA Repair; DNA, Bacterial/metabolism; DNA, Single-Stranded/metabolism; Escherichia coli/enzymology; Exodeoxyribonucleases/drug effects; Exodeoxyribonucleases/genetics; Exodeoxyribonucleases/metabolism; Exoribonucleases/drug effects; Exoribonucleases/genetics; Exoribonucleases/metabolism; Magnesium/pharmacology; Recombinant Proteins/metabolism; Substrate Specificity |
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