Phosphorylation of large tumour antigen by cdc2 stimulates SV40 DNA replication

Simian virus 40 large tumour antigen (T) is a replication origin binding protein required for viral DNA synthesis. Unphosphorylated T antigen is deficient in promoting DNA replication in vitro but can be activated by phosphorylation at residue threonine 124 by the cdc2 protein kinase. This observati...

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Bibliographic Details
Published in:Nature (London) 1989-10, Vol.341 (6242), p.503-507
Main Authors: McVey, Duncan, Brizuela, Leonardo, Mohr, Ian, Marshak, Daniel R, Gluzman, Yasha, Beach, David
Format: Article
Language:English
Subjects:
Antigens, Polyomavirus Transforming - genetics
Antigens, Polyomavirus Transforming - isolation & purification
Biological and medical sciences
CDC2 Protein Kinase
Deoxyribonucleic acid
DNA
DNA Replication
DNA-Binding Proteins - metabolism
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
HeLa Cells - enzymology
Humans
Kinetics
Medical research
Molecular and cellular biology
Molecular genetics
Phosphoproteins - metabolism
Phosphorylation
Protein Kinases - metabolism
Replication
Simian virus 40
Simian virus 40 - genetics
Simian virus 40 - immunology
Viruses
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Summary:Simian virus 40 large tumour antigen (T) is a replication origin binding protein required for viral DNA synthesis. Unphosphorylated T antigen is deficient in promoting DNA replication in vitro but can be activated by phosphorylation at residue threonine 124 by the cdc2 protein kinase. This observation demonstrates that T is regulated by phosphorylation and provides a model for cdc2 function in the control of DNA replication.
ISSN:0028-0836
1476-4687
DOI:10.1038/341503a0