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PMID: 8670419 Published · ppublish English Journal Article

Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain.

Science (New York, N.Y.) ·Vol. 273 ·No. 5276 ·1996-08-09 ·Pages 794-7

Xu X, Sun YL, Hoey T

Abstract

STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of STAT proteins was required for cooperative DNA binding, although this domain was not essential for dimerization or binding to a single site. Cooperative binding interactions enabled the STAT proteins to recognize variations of the consensus site. These sites can be specific for the different STAT proteins and may function to direct selective transcriptional activation.

MeSH Terms
Animals Base Sequence Binding Sites Cell Line DNA/metabolism DNA-Binding Proteins/chemistry,immunology,metabolism Interferon-gamma/genetics Introns Molecular Sequence Data Mutation Oligodeoxyribonucleotides/metabolism Promoter Regions, Genetic STAT1 Transcription Factor STAT4 Transcription Factor Sequence Deletion Signal Transduction Trans-Activators/chemistry,immunology,metabolism Transcriptional Activation
Chemicals
DNA-Binding Proteins Oligodeoxyribonucleotides STAT1 Transcription Factor STAT4 Transcription Factor Trans-Activators Interferon-gamma DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Xu X
Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.
Sun Y L
Hoey T
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1996-08-09
Pages
794-7
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Databases
GENBANK
L78440
Corrections
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