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Negative regulation of Sp1 trans-activation is correlated with the binding of cellular proteins to the amino terminus of the Sp1 trans-activation domain. J Biol Chem 1994 Aug 12;269(32):20674-81

Date

08/12/1994

Pubmed ID

8051168

Scopus ID

2-s2.0-0028043272 (requires institutional sign-in at Scopus site)   115 Citations

Abstract

Sp1 is a well characterized and ubiquitously expressed transcription factor that regulates the constitutive and induced expression of a variety of mammalian genes. It is unclear whether Sp1 activity is regulated in vivo; the mechanism by which Sp1 interacts with the basal transcription complex has not been firmly established. We report the identification of a ubiquitously expressed and evolutionarily conserved nuclear protein, p74, that specifically binds Sp1 in vivo and in vitro. p74 interacts with several portions of the Sp1 trans-activation domain in vitro, and we correlate the binding of p74 to the amino-terminal serine/threonine-rich subdomain of Sp1 with the inhibition of Sp1-mediated transcription in vivo.

Author List

Murata Y, Kim HG, Rogers KT, Udvadia AJ, Horowitz JM

Author

Ava Udvadia BS,PhD Associate Professor in the Biological Sciences department at University of Wisconsin - Milwaukee




MESH terms used to index this publication - Major topics in bold

Binding Sites
Cells, Cultured
DNA-Binding Proteins
Fungal Proteins
Nuclear Proteins
Recombinant Fusion Proteins
Saccharomyces cerevisiae Proteins
Sp1 Transcription Factor
Transcription Factors
Transcription, Genetic
Transcriptional Activation