Functional dissection of TFIIN domains required for TFIIb-TFIID-promoter complex formation and basal transcription activity

Article Abstract:

An analysis of the complex formation and basal transcription of TFIIB was undertaken with the application deletion mutants in a systematic series. The structure of the D-B-DNA complex was observed with the electrophetic mobility shift assay using purified human TFIID tau and TFIIB. Results showed that the C-terminal domain was essential and adequate for the D-DNA-complex interaction. On the other hand, the N-terminal domain was necessary for the activation of basal transcription initiation. The similarities ofTFIIB and TFIID tau functions have also been discussed.

Protein synthesis, Protein biosynthesis

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Crystal structure of a TFIIB-TBP-TATA-element ternary complex

Article Abstract:

The core structure of TFIIB-TBP-TATA-element ternary complex consists of a two-domain alpha-helical protein resembling a cyclin A, shows activity with the C-terminal stirrup of TATA box-binding protein and interfaces with the phosphoribose core promoter at both the ends of the TATA element as revealed at 2.7 angstroms resolution. TFIIB may be affecting the activities of the kinase and cyclin subunits of TFIIH or other cyclin dependent kinases as suggested by the similarity of cTFIIB and cyclin A.

Analysis, DNA binding proteins

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The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1

Article Abstract:

Previous research findings indicate that subunits of the transcription factor TFIID other than the TATA-binding polypeptide must be essential cofactors and potential targets for activators. A 250K subunit of TFIID was identified and found to be identical to a gene product that has been implicated in progression through the late G1 phase of the cell cycle. The findings suggest that a portion of p250 may play a role in the activation of a subset of genes essential to cell cycle progression.

Cell cycle

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