Large T antigens of many polyomaviruses are able to form complexes with the retinoblastoma protein.
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.
Dyson
N
N
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
Bernards
R
R
Friend
S H
SH
Gooding
L R
LR
Hassell
J A
JA
Major
E O
EO
Pipas
J M
JM
Vandyke
T
T
Harlow
E
E
D000595:Amino Acid Sequence; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000032:analysis / Q000235:genetics; D000882:Haplorhini; D006801:Humans; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D010215:Papio; D010750:Phosphoproteins / Q000032:analysis / Q000378:metabolism; D011120:Polyomavirus / Q000235:genetics / Q000276:immunology*; D011485:Protein Binding; D016160:Retinoblastoma Protein; D012689:Sequence Homology, Nucleic Acid
D000952:Antigens, Polyomavirus Transforming; D009687:Nuclear Proteins; D010750:Phosphoproteins; D016160:Retinoblastoma Protein