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PMID: 1654462 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The T/t common region of simian virus 40 large T antigen contains a distinct transformation-governing sequence.

Journal of virology ·Vol. 65 ·No. 10 ·1991-10-00 ·Pages 5647-52

Marsilio E, Cheng SH, Schaffhausen B, Paucha E, Livingston DM

Abstract

Simian virus 40 large T antigen (T) can transform cultured cells, but the mechanisms by which it functions are not entirely understood. Several lines of evidence have suggested that the amino-terminal approximately 130 residues of T may be sufficient to confer the transforming capability. Oligonucleotide-directed mutagenesis was used to generate a series of deletion and substitution mutants within the amino-terminal 82 residues of T, the segment which is shared with simian virus 40 small t antigen (t). Results of stability and transformation assays of these mutants strongly suggest that the 1-to-82 region of T contains sequences which govern T transforming activity and affect in vivo stability. Instability and a defect in transforming activity could be separated from one another genetically. Thus, the 1-to-82 region appears to contain a specific region that contributes to the transforming function of the protein. This segment operates by means other than the simple binding of pRb and/or p107.

MeSH Terms
Animals Antigens, Polyomavirus Transforming/genetics,isolation & purification,physiology Blotting, Western Cell Line Cell Transformation, Neoplastic Chromosome Deletion Mice Simian virus 40/genetics
Chemicals
Antigens, Polyomavirus Transforming
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Marsilio E
Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
Cheng S H
Schaffhausen B
Paucha E
Livingston D M
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.65.10.5647-5652.1991
Published
1991-10-00
Pages
5647-52
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC249088
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.65.10.5647-5652.1991 PMC Full Text View journal details
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