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PMID: 2144363 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Presence of a potent transcription activating sequence in the p53 protein.

Science (New York, N.Y.) ·Vol. 249 ·No. 4972 ·1990-08-31 ·Pages 1046-9

Fields S, Jang SK

Abstract

The p53 gene is frequently mutated in a wide variety of human cancers. However, the role of the wild-type p53 gene in growth control is not known. Hybrid proteins that contain the DNA binding domain of yeast GAL4 and portions of p53 have been used to show that the p53 protein contains a transcription-activating sequence that functions in both yeast and mammalian cells. The NH2-terminal 73 residues of p53 activated transcription in mammalian cells as efficiently as the herpes virus protein VP16, which contains one of the strongest known activation domains. Combined with previous data that showed p53 is localized to the nucleus and can bind to DNA, these results support the idea that one function of p53 is to activate the transcription of genes that suppress cell proliferation.

MeSH Terms
Animals Cell Line Genetic Vectors Models, Genetic Nuclear Proteins/genetics Oncogene Proteins/genetics,metabolism Phosphoproteins/genetics,metabolism RNA, Messenger/genetics Saccharomyces cerevisiae/genetics Suppression, Genetic Transcription Factors/genetics Transcription, Genetic Tumor Suppressor Protein p53 beta-Galactosidase/genetics,metabolism
Chemicals
Nuclear Proteins Oncogene Proteins Phosphoproteins RNA, Messenger Transcription Factors Tumor Suppressor Protein p53 beta-Galactosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fields S
Department of Microbiology, School of Medicine, State University of New York, Stony Brook 11794.
Jang S K
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1990-08-31
Pages
1046-9
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIAID NIH HHS · 2R37 AI15122 · United States
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