The ability to associate with activation domains in vitro is not required for the TATA box-binding protein to support activated transcription in vivo

Tansey, W. P., Herr, W. (November 1995) The ability to associate with activation domains in vitro is not required for the TATA box-binding protein to support activated transcription in vivo. Proc Natl Acad Sci U S A, 92 (23). pp. 10550-4. ISSN 0027-8424 (Print)

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URL: http://www.ncbi.nlm.nih.gov/pubmed/7479838

Abstract

The TATA box-binding protein (TBP) interacts in vitro with the activation domains of many viral and cellular transcription factors and has been proposed to be a direct target for transcriptional activators. We have examined the functional relevance of activator-TBP association in vitro to transcriptional activation in vivo. We show that alanine substitution mutations in a single loop of TBP can disrupt its association in vitro with the activation domains of the herpes simplex virus activator VP16 and of the human tumor suppressor protein p53; these mutations do not, however, disrupt the transcriptional response of TBP to either activation domain in vivo. Moreover, we show that a region of VP16 distinct from its activation domain can also tightly associate with TBP in vitro, but fails to activate transcription in vivo. These data suggest that the ability of TBP to interact with activation domains in vitro is not directly relevant to its ability to support activated transcription in vivo.

Item Type: Paper
Uncontrolled Keywords: Comparative Study DNA-Binding Proteins/genetics/ metabolism Herpes Simplex Virus Protein Vmw65/ metabolism Humans Models, Molecular Point Mutation Protein Binding Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Structure-Activity Relationship TATA-Box Binding Protein Transcription Factors/genetics/ metabolism Transcription, Genetic Tumor Suppressor Protein p53/ metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
organism description > virus > herpes simplex virus
organism description > animal > mammal > primates > hominids > human
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Herr lab
CSHL labs > Tansey lab
Depositing User: Jessica Koos
Date: 7 November 1995
Date Deposited: 12 Aug 2014 15:45
Last Modified: 09 Nov 2017 19:23
PMCID: PMC40649
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30646

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