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PMID: 75271 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Reverse transcriptase of RNA tumor viruses. V. In vitro proteolysis of reverse transcriptase from avian myeloblastosis virus and isolation of a polypeptide manifesting only RNase H activity.

Journal of virology ·Vol. 25 ·No. 2 ·1978-02-00 ·Pages 652-63

Lai MH, Verma IM

Abstract

Purified avian myeloblastosis virus reverse transcriptase contains two subunits that are structurally related. The large subunit, beta (molecular weight, 95,000), was converted in vitro by chymotrypsin into a polypeptide of molecular weight 63,000. This polypeptide was indistinguishable from the small subunit, alpha (molecular weight, 65,000), in its chromatographic behavior on the phosphocellulose column and its tryptic peptide composition. During this proteolytic conversion, a polypeptide of molecular weight 32,000 (fragment B) was obtained. It was composed of tryptic peptides unique to beta and appeared to be derived from the portion of the beta subunit that was cleaved off during the conversion of beta into alpha. Upon continued proteolysis, a smaller polypeptide of molecular weight 24,000 (fragment A) was generated. This polypeptide manifested only RNase H activity and shared common amino acid sequences with beta and alpha subunits. Fragment A did not share any amino acid sequence homology with fragment B.

MeSH Terms
Avian Leukosis Virus/enzymology Avian Myeloblastosis Virus/enzymology Chymotrypsin/metabolism Molecular Weight Peptides/analysis,isolation & purification RNA-Directed DNA Polymerase/analysis,metabolism Ribonucleases/metabolism
Chemicals
Peptides RNA-Directed DNA Polymerase Ribonucleases Chymotrypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lai M H
Verma I M
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42 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1978-02-00
Pages
652-63
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC353978
Subset
IM
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