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PMID: 2154613 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Large T antigens of many polyomaviruses are able to form complexes with the retinoblastoma protein.

Journal of virology ·Vol. 64 ·No. 3 ·1990-03-00 ·Pages 1353-6

Dyson N, Bernards R, Friend SH, Gooding LR, Hassell JA, Major EO, Pipas JM, Vandyke T, Harlow E

Abstract

Stable protein complexes between the large T antigens of mouse, monkey, baboon, or human polyomaviruses and the retinoblastoma protein were detected by an in vitro coimmunoprecipitation assay. All of the large T antigens tested were able to bind to both human and mouse retinoblastoma polypeptides, showing that these interactions have been conserved during evolution.

MeSH Terms
Amino Acid Sequence Animals Antigens, Polyomavirus Transforming/analysis,genetics Haplorhini Humans Molecular Sequence Data Nuclear Proteins Papio Phosphoproteins/analysis,metabolism Polyomavirus/genetics,immunology Protein Binding Retinoblastoma Protein Sequence Homology, Nucleic Acid
Chemicals
Antigens, Polyomavirus Transforming Nuclear Proteins Phosphoproteins Retinoblastoma Protein
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Dyson N
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
Bernards R
Friend S H
Gooding L R
Hassell J A
Major E O
Pipas J M
Vandyke T
Harlow E
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.64.3.1353-1356.1990
Published
1990-03-00
Pages
1353-6
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC249255
Subset
IM
Grants
NCI NIH HHS · CA14106 · United States
External Links
PubMed source DOI: 10.1128/JVI.64.3.1353-1356.1990 PMC Full Text View journal details
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