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PMID: 2936897 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Identification and characterization of a protein covalently bound to DNA of minute virus of mice.

Journal of virology ·Vol. 57 ·No. 3 ·1986-03-00 ·Pages 1094-104

Chow M, Bodnar JW, Polvino-Bodnar M, Ward DC

Abstract

We identified a protein which is covalently linked to a fraction of the DNA synthesized in cells infected with minute virus of mice. This protein is specifically bound to the 5' terminus of the extended terminal conformers of the minute virus of mice replicative-form DNA species and of a variable fraction of single-stranded viral DNA. The chemical stability of the protein-DNA linkage is characteristic of a phosphodiester bond between a tyrosine residue in the protein and the 5' end of the DNA. The terminal protein (TP) bound on all DNA forms has a relative molecular weight of 60,000; it is also seen free in extracts from infected cells. Immunologic comparison of the TP with the other known viral proteins suggests that the TP is not related to the capsid proteins or NS-1.

MeSH Terms
Animals Cross Reactions DNA Replication DNA, Viral/analysis,isolation & purification Electrophoresis, Polyacrylamide Gel Filtration Guinea Pigs Immune Sera/immunology Minute Virus of Mice/analysis,genetics Molecular Weight Parvoviridae/genetics Viral Nonstructural Proteins Viral Proteins/analysis,immunology,isolation & purification Viral Structural Proteins Virus Replication
Chemicals
DNA, Viral Immune Sera Viral Nonstructural Proteins Viral Proteins Viral Structural Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chow M
Bodnar J W
Polvino-Bodnar M
Ward D C
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60 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.57.3.1094-1104.1986
Published
1986-03-00
Pages
1094-104
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC252843
Subset
IM
Grants
NIAID NIH HHS · AI-19973 · United States
NCI NIH HHS · CA-16038 · United States
External Links
PubMed source DOI: 10.1128/JVI.57.3.1094-1104.1986 PMC Full Text View journal details
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