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PMID: 2170980 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Simian virus 40 small tumor antigen and an amino-terminal domain of large tumor antigen share a common transforming function.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 19 ·1990-10-00 ·Pages 7448-52

Montano X, Millikan R, Milhaven JM, Newsom DA, Ludlow JW, Arthur AK, Fanning E, Bikel I, Livingston DM

Abstract

The 82-residue amino-terminal sequences of simian virus 40 large tumor antigen (TAg) and small tumor antigen (tAg) are identical. Genetic analysis of TAg lacking amino acids 1-82 revealed that it was transformation-defective, as revealed by the agar growth assay, except when introduced in the presence of tAg. Since the latter, alone, lacks overt transforming activity, it would appear that the function of the sequence common to TAg and tAg is necessary, but not sufficient, for TAg transforming activity and that tAg can provide that function or its equivalent in trans. Thus, tAg may, in part, be viewed as a "portable" copy of a TAg functional domain.

MeSH Terms
Animals Antigens, Polyomavirus Transforming/genetics Base Sequence Cell Line Cell Transformation, Neoplastic Clone Cells Mice Mice, Inbred BALB C Molecular Sequence Data Oligonucleotide Probes Plasmids Simian virus 40/genetics Transfection
Chemicals
Antigens, Polyomavirus Transforming Oligonucleotide Probes
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Montano X
Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.
Millikan R
Milhaven J M
Newsom D A
Ludlow J W
Arthur A K
Fanning E
Bikel I
Livingston D M
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30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.19.7448
Published
1990-10-00
Pages
7448-52
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54764
Subset
IM
Grants
NCI NIH HHS · CA24715 · United States
External Links
PubMed source DOI: 10.1073/pnas.87.19.7448 PMC Full Text View journal details
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