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PMID: 3554236 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Homology between the DNA-binding domain of the GCN4 regulatory protein of yeast and the carboxyl-terminal region of a protein coded for by the oncogene jun.

Vogt PK, Bos TJ, Doolittle RF

Abstract

The product of the recently described oncogene jun shows significant amino acid sequence homology with the GCN4 yeast transcriptional activator protein. The similarity is restricted to the 66 carboxyl-terminal amino acids, thought to be the DNA-binding domain of the GCN4 protein. In these alpha-helix-permissive regions of the jun and GCN4 products there is also a lesser but still significant amino acid resemblance to the fos protein and a marginal degree of similarity to myc proteins. The amino acid sequence homology between GCN4 and jun gene products suggests that the jun protein may bind to DNA in a sequence-specific way and exert a regulatory function.

MeSH Terms
Amino Acid Sequence Binding Sites DNA/metabolism DNA-Binding Proteins Fungal Proteins/genetics Genes, Fungal Humans Oncogenes Protein Kinases Proto-Oncogene Proteins/genetics Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins Sequence Homology, Nucleic Acid Transcription Factors/genetics ras Proteins
Chemicals
DNA-Binding Proteins Fungal Proteins Proto-Oncogene Proteins Saccharomyces cerevisiae Proteins Transcription Factors DNA Protein Kinases ras Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Vogt P K
Bos T J
Doolittle R F
References (16)
16 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
Published
1987-05-00
Pages
3316-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304860
Subset
IM
Grants
NCI NIH HHS · CA 13213 · United States
NCI NIH HHS · CA 29777 · United States
NCI NIH HHS · CA 42564 · United States
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