Enzyme from Calf Thymus Degrading the RNA Moiety of DNA-RNA Hybrids: Effect on DNA-Dependent RNA Polymerase

@article{Stein1969EnzymeFC,
  title={Enzyme from Calf Thymus Degrading the RNA Moiety of DNA-RNA Hybrids: Effect on DNA-Dependent RNA Polymerase},
  author={Hans Stein and Peter Hausen},
  journal={Science},
  year={1969},
  volume={166},
  pages={393 - 395}
}
An enzyme present in extracts from calf thymus degrades specifically the RNA moiety of DNA-RNA hybrids. Other nucleic acids, such as single- or double-stranded DNA and single- or double-stranded RNA, are not affected to a comparable degree. If prepared free of the hybrid-degrading enzyme, RNA polymerase from calf thymus shows a fivefold increase in activity on denatured DNA as compared to native DNA. 
Association of the viral reverse transcriptase with an enzyme degrading the RNA moiety of RNA-DNA hybrids.
TLDR
This work has demonstrated that RNA-DNA hybrids have been demonstrated to occur as intermediates in this reaction and single stranded DNA is generated as an early reaction product, which is then replicated to give a double stranded DNA product.
Calf thymus RNA polymerases exhibit template specificity.
A factor from calf thymus stimulating DNA-dependent RNA polymerase isolated from this tissue.
A large scale purification procedure of RNA polymerase from calf thymus is described. A factor stimulating synthesis of RNA by this enzyme has been extracted from the same tissue. Addition of the
A distinct form of ribonuclease H from calf thymus stimulates its homologous DNA-polymerase-alpha-primase complex.
TLDR
A ribonuclease H which degrades RNA specifically in RNA-DNA hybrids and stimulates its homologous DNA-polymerase-primase complex was purified from calf thymus and is a likely candidate for a genuine primer-removing enzyme in mammalian cells.
A nuclease from animal serum which hydrolyzes double-stranded RNA.
  • R. Stern
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 1970
Role of DNA · RNA Hybrids in Eukaryotes Purification of Two Ribonucleases H from Yeast Cells
Two ribonucleases H, which specifically degrade RNA in RNA-DNA hybrid structures, have been extensively purified from extracts of Saccharomyces corevisiae. Ribonuclease H1 can be obtained in high
Ribonuclease H activity present in purified DNA polymerase from avian myeloblastosis virus.
Site specific enzymatic cleavage of RNA
TLDR
The hybridization of a DNA oligonucleotide a specific tetramer or longer will direct a cleavage by RNase H to a specific site in RNA, which can then be labeled at their 5' or 3' ends, purified, and sequenced directly.
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A Predoctoral Research Fellow of the U.S. Public Health Service, these PROCEEDINGS, 48, 859 (1962) are presented.
Further recent experiments have shown that the enzyme described above degrades polyuridylic acid if it is hybridized to polydeoxyadenylic acid but not if it is hybridized to polyadenylic acid
  • This further demonstrates the specificity of the enzyme. HANS STEIN PETER HAUSEN Afax-PlFlack-hIstitut fiir Biologie, A bteilung Beerm-eaina?, Tiibingeni, Speinatn nstrasse 34, West Germaniy References and Notes 1. C. F. Fox and S. B. Weiss, J. Biol. Chze,n. 239, 175 ( 1964): J. S. Krakow and S. Och
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Wandel for technical assistance. We thank Dr. H. Schaller for labeled and tinlabeled bacteriophage fd DNA and Dr. P. H. Hofschneider, for the labeled MS2-RF