TAFII55 binding to TAFII250 inhibits its acetyltransferase activity
نویسندگان
چکیده
منابع مشابه
The TAFII250 Subunit of TFIID Has Histone Acetyltransferase Activity
The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltr...
متن کاملCK2 phosphorylates SSRP1 and inhibits its DNA-binding activity.
We have previously shown that CK2 associates with the human high-mobility group protein SSRP1 and that this association increases in response to UV irradiation. CK2 also phosphorylates SSRP1 in vitro. Here we extend this work by investigating CK2 regulation of SSRP1 function through phosphorylation. Phosphorylation of SSRP1 by CK2 inhibited the nonspecific DNA-binding activity of SSRP1 and FACT...
متن کاملGambogic acid inhibits the catalytic activity of human topoisomerase IIalpha by binding to its ATPase domain.
This study is intended to characterize the cellular target of gambogic acid (GA), a natural product isolated from the gamboge resin of Garcinia hurburyi tree, which possesses potent in vitro and in vivo antitumor activities. The antiproliferative activity of GA was further confirmed here in a panel of human tumor cells and multidrug-resistant cells. We found that GA significantly inhibited the ...
متن کاملZn2+ inhibits the anion transport activity of band 3 by binding to its cytoplasmic tail.
Zn2+ can induce a conformational change of Band 3 with concomitant inhibition of its anion transport activity of human erythrocyte membrane vesicles only from the cytoplasmic side. The Zn2+ inhibition exhibits a dose-dependent manner with an apparent half maximal concentration of 50 microM ZnCl2 and can be reversed by 0.5 mM EDTA, but not by 1 mM dithiothreitol. The Zn2+ effect is specific and ...
متن کاملFactor-specific modulation of CREB-binding protein acetyltransferase activity.
CREB-binding proteins (CBP) and p300 are essential transcriptional coactivators for a large number of regulated DNA-binding transcription factors, including CREB, nuclear receptors, and STATs. CBP and p300 function in part by mediating the assembly of multiprotein complexes that contain additional cofactors such as p300/CBP interacting protein (p/CIP), a member of the p160/SRC family of coactiv...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2001
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.211444798