TAFII55 binding to TAFII250 inhibits its acetyltransferase activity
AUTOR(ES)
Gegonne, Anne
FONTE
The National Academy of Sciences
RESUMO
The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. One of the TAFs, TAFII250, has acetyltransferase (AT) activity that is necessary for transcription of MHC class I genes: inhibition of the AT activity represses transcription. To identify potential cellular factors that might regulate the AT activity of TAFII250, a yeast two-hybrid library was screened with a TAFII250 segment (amino acids 848-1279) that spanned part of its AT domain and it's the domain that binds to the protein, RAP74. The TFIID component, TAFII55, was isolated and found to interact predominantly with the RAP74-binding domain. TAFII55 binding to TAFII250 inhibits its AT activity. Importantly, the addition of recombinant TAFII55 to in vitro transcription assays inhibits TAFII250-dependent MHC class I transcription. Thus, TAFII55 is capable of regulating TAFII250 function by modulating its AT activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=60071Documentos Relacionados
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