Article
The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity.
RNA (New York, N.Y.) - 1 May 1995
Cerritelli S M, Crouch R J
Abstract excerpt
Eukaryotic ribonucleases H of known sequence are composed of an RNase H domain similar in size and sequence to that of Escherichia coli RNase HI and additional domains of unknown function. The RNase H1 of Saccharomyces cerevisiae has such an RNase H domain at its C-terminus. Here we show that the N-terminal non-RNase H portion of the yeast RNase H1 binds tightly to double-stranded RNA (dsRNA) and RNA-DNA hybrids...
Topics
- Amino Acid Sequence
- Binding Sites
- Gene Expression Regulation, Enzymologic
- Magnesium
- Molecular Sequence Data
- Mutation
- Nucleic Acid Heteroduplexes
- Poly I-C
- Protein Binding
- RNA, Double-Stranded