NDLI: Ribonuclease H activities associated with viral reverse transcriptases are endonucleases.

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OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins.

Ribonuclease H activities associated with viral reverse transcriptases are endonucleases.

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Specific photoaffinity labeling of two plasma membrane polypeptides with an azido auxin.

Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precede growth changes in maize seedlings.

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Ribonuclease H activities associated with viral reverse transcriptases are endonucleases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Krug, M. S. Berger, S. L.
Description	Author Affiliation: Krug MS ( Division of Cancer Biology and Diagnosis, National Cancer Institute, Bethesda, MD 20892.);
Abstract	A series of test substrates have been synthesized to establish the effect of termini on the putative exoribonuclease H activity of reverse transcriptase. Recombinant reverse transcriptase from human immunodeficiency virus, natural enzyme from avian myeloblastosis virus, and a known endonuclease, Escherichia coli ribonuclease H, cleaved relaxed, circular, covalently closed plasmids in which 770 consecutive residues of one strand were ribonucleotides. The avian enzyme also deadenylated capped globin mRNA with a covalently attached oligo(dT) tail at the 3' end. These results resolve a long-standing controversy--that the viral enzymes are obligatory exonucleases in vitro, based on their failure to cleave certain substrates for E. coli ribonuclease H, including circular poly(A).linear poly(T) and ribonucleotide-substituted supercoiled plasmids, but resemble endonucleases in vivo, based on their ability to degrade RNA in complex DNA.RNA hybrids. The data strongly suggest that the viral enzymes are endonucleases with exquisite sensitivity to the conformation of heteroduplexes. Inhibition of viral, but not cellular, ribonuclease H with ribonucleoside-vanadyl complexes further distinguishes these enzymes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endoribonucleases Metabolism RNA-Directed DNA Polymerase Avian Myeloblastosis Virus Enzymology Antagonists & Inhibitors Escherichia Coli HIV RNA, Messenger Reverse Transcriptase Inhibitors Ribonuclease H Structure-Activity Relationship Substrate Specificity Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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