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Nucleic Acids Research, 1978, Vol. 5, No. 11 4245-4262
© 1978

Articles

T7 gene 6 exonuclease has an RNase H activity

Kazuo Shinozaki{dagger} and Okazaki Tuneko*

Institute of Molecular Biology, Faculty of Science, Nagoya University Nagoya, 464, Japan

*To whom correspondence should be addressed

Received September 8, 1978.

T7 gene 6 exonuclease has been shown to have an RNase H activity as well as a double-strand specific DNase activity by the following experiments: The RNase H activity coelutes with the DNase activity from DEAR-cellulose, phosphocellulose, hydroxyapatite, and Sephadex G-200 columns. Gene 6 exonuclease specified by a T7 strain with a temperature sensitive mutation in gene 6 has an extremely heat-labile RNase H activity as well as a heat-labile DNase activity. T7 gene 6 exonuclease degrades the RNA region of a poly(A).poly(dT) hybrid polymer exonucleolytically from the 5' terminus, releasing a ribonucleoside 5'-monophosphate product. When the RNA strand of a {varphi}X174 RNA.DNA hybrid molecule synthesized with E. coli RNA polymerase is degraded, a ribonucleoside triphosphate is produced from the 5'-triphosphate terminus. Participation of T7 gene 6 exonuclease in the removal of primer RNA in discontinuous replication of T7 DNA is discussed.

{dagger}Present address: National Institute of Genetics, Mishima 411, Japan


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