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 WP, Herr W
Proc Natl Acad Sci U S A. 1995 92 (23): 10550-4

PMID: 7479838 · PMCID: PMC40649 · DOI:10.1073/pnas.92.23.10550

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.

MeSH Terms (11)

DNA-Binding Proteins Herpes Simplex Virus Protein Vmw65 Humans Models, Molecular Point Mutation Protein Binding Structure-Activity Relationship TATA-Box Binding Protein Transcription, Genetic Transcription Factors Tumor Suppressor Protein p53

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