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Publication : TAFII55 binding to TAFII250 inhibits its acetyltransferase activity.

First Author  Gegonne A Year  2001
Journal  Proc Natl Acad Sci U S A Volume  98
Issue  22 Pages  12432-7
PubMed ID  11592977 Mgi Jnum  J:149201
Mgi Id  MGI:3847877 Doi  10.1073/pnas.211444798
Citation  Gegonne A, et al. (2001) TAFII55 binding to TAFII250 inhibits its acetyltransferase activity. Proc Natl Acad Sci U S A 98(22):12432-7
abstractText  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, TAF(II)250, 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 TAF(II)250, a yeast two-hybrid library was screened with a TAF(II)250 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, TAF(II)55, was isolated and found to interact predominantly with the RAP74-binding domain. TAF(II)55 binding to TAF(II)250 inhibits its AT activity. Importantly, the addition of recombinant TAF(II)55 to in vitro transcription assays inhibits TAF(II)250-dependent MHC class I transcription. Thus, TAF(II)55 is capable of regulating TAF(II)250 function by modulating its AT activity.
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