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
08/12/1994Pubmed ID
8051168Scopus ID
2-s2.0-0028043272 (requires institutional sign-in at Scopus site) 115 CitationsAbstract
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 JMAuthor
Ava Udvadia BS,PhD Associate Professor in the Biological Sciences department at University of Wisconsin - MilwaukeeMESH terms used to index this publication - Major topics in bold
Binding SitesCells, Cultured
DNA-Binding Proteins
Fungal Proteins
Nuclear Proteins
Recombinant Fusion Proteins
Saccharomyces cerevisiae Proteins
Sp1 Transcription Factor
Transcription Factors
Transcription, Genetic
Transcriptional Activation