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Article

Strong nucleic acid binding to the Escherichia coli RNase HI mutant with two arginine residues at the active site.

Biochimica et biophysica acta - 5 May 2001

Tsunaka Y, Haruki M, Morikawa M, Kanaya S

Abstract excerpt

The biochemical properties of the mutant protein D10R/E48R of Escherichia coli RNase HI, in which Asp(10) and Glu(48) are both replaced by Arg, were characterized. This mutant protein has been reported to have metal-independent RNase H activity at acidic pH [Casareno et al. (1995) J. Am. Chem. Soc. 117, 11011-11012]. The far- and near-UV CD spectra of this mutant protein were similar to those of the wild-type...

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PMID: 11343799
DOI: 10.1016/s0167-4838(01)00180-7

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