The VP16 activation domain interacts with multiple transcriptional components as determined by protein-protein cross-linking in vivo

  • Hall D
  • Struhl K
  • 147


    Mendeley users who have this article in their library.
  • 98


    Citations of this article.


Transcriptional activator proteins recruit the RNA polymerase II machinery and chromatin-modifying activities to promoters. Biochemical experiments indicate that activator proteins can associate with a large number of proteins, and many such proteins have been proposed to be direct targets of activators. However, there is great uncertainty about which biochemical interactions are physiologically relevant. Here, we develop a formaldehyde-based cross-linking procedure to identify protein-protein interactions that occur under physiological conditions. We show that the VP16 activation domain directly interacts with TATA-binding protein (TBP), TFIIB, and the SAGA histone acetylase complex in vivo.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Daniel B. Hall

  • Kevin Struhl

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free