Negative regulation of Sp1 trans-activation is correlated with the binding of cellular proteins to the amino terminus of the Sp1 trans-activation domain

Autor:	Y, Murata, H G, Kim, K T, Rogers, A J, Udvadia, J M, Horowitz
Rok vydání:	1994
Předmět:	DNA-Binding Proteins Fungal Proteins Transcriptional Activation Binding Sites Saccharomyces cerevisiae Proteins Transcription Genetic Sp1 Transcription Factor Recombinant Fusion Proteins Nuclear Proteins Cells Cultured Transcription Factors
Zdroj:	The Journal of biological chemistry. 269(32)
ISSN:	0021-9258
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::32fcc277f25465bcb83152ded69597b2 https://pubmed.ncbi.nlm.nih.gov/8051168 Zobrazit plný text záznamu