Rb interacts with TAF(II)250/TFIID through multiple domains

Zhaohui Shao, Jennifer L. Siegert, Siegfried Ruppert, Paul D. Robbins

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


The retinoblastoma tumor suppressor gene product (Rb) binds directly to the largest TFIID subunit, TATA-binding protein associated factor TAF(II)250, first identified as the cell cycle regulatory protein CCG1. Here we map the domains in Rb and TAF(II)250 important for their interaction in vitro and in vivo. Both the amino terminus and the large pocket of Rb are able to associate independently with TAF(II)250. The binding domain(s) within the large pocket are distinct from the viral oncoprotein and E2F binding region since certain pocket mutations, which abolish E1A binding, do not abolish TAF(II)250 binding. Consistent with the large pocket of Rb binding to TAF(II)250, the large pocket domains of both p107 and p130 are able to bind to TAF(II)250 in vivo. We also demonstrate that at least two regions of TAF(II)250 are able to bind to the large pocket of Rb independently whereas the amino terminus of Rb binds to a distinct domain in TAF(II)250. We further demonstrate that Rb can bind to TFIID in vitro, presumably in part through an interaction with TAF(II)250. Our results suggest a complex interaction between Rb and TAF(II)250 and imply that TAF(II)250, TFIID, and potentially other basal transcription factors are targets for regulation by Rb and Rb-related proteins.

Original languageEnglish (US)
Pages (from-to)385-392
Number of pages8
Issue number4
StatePublished - 1997
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported in part by a public health service grant 55227 from the National Cancer Institute to PDR. The authors would like to thank Dr John Rushton for his technical assistance in the preparation of this manuscript and Dr Robert Tjian for his support during the course of this work.


  • Protein-protein interaction
  • Retinoblastoma protein
  • Transcription factor TFIID


Dive into the research topics of 'Rb interacts with TAF(II)250/TFIID through multiple domains'. Together they form a unique fingerprint.

Cite this