期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：11
页码：3360-3364
DOI：10.1073/pnas.69.11.3360
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Ribonuclease H from human KB cells, chick embryos, calf thymus, avian myeloblastosis virus, and Rous associated virus specifically degrades the RNA of DNA{middle dot}RNA hybrids, producing mono- and oligoribonucleotides terminated in 5'-phosphates. The cellular RNase H is an endonuclease, whereas the viral enzyme appears to be an exonuclease. Viral DNA polymerase and RNase H copurify through all separation steps. Therefore, RNase H activity is an intrinsic part of the viral DNA polymerase. DNA{middle dot}RNA hybrids are also degraded by nucleases associated with cellular DNA polymerases and by exonuclease III. However, these nucleases differ from RNase H in their ability to degrade both strands of DNA{middle dot}RNA hybrids.
