Deviant TATA-box binding protein

Article Abstract:

The structure of the C-terminal domains of TATA-box binding protein (TBP) proteins reported by D.B. Nikolov and his colleagues is suggested to be universal to all TBP DNA-binding domains. But the human malaria parasite Plasmodium falciparum has a TBP homologue that is very different. The difference between this molecule and the corresponding one in the human host might reflect functional differences that could be exploited in the treatment of malaria.

Proteins, Protein structure

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A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein

Article Abstract:

Genetic and biochemical studies of yeast protein indicate the occurrence of binding between the activation domain (AD) of the regulatory protein Gal4 and Sug1, a yeast protein, which also binds to herpes virus VP16. Sug1, which is a type of highly conserved ATPase, exhibits correlation with the TATA-binding protein. These studies suggest Sug1 to be a mediator protein and ATP hydrolysis to be a part of transcriptional initiation.

Adenosine triphosphatase

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Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor

Article Abstract:

Yeast interaction assay reveals that the transcriptional activator, serum response factor (SRF), binds the transcription factor TFIIB at the RAP74 subunit. The binding occurs specifically between the central charged cluster domain of RAP74 subunit and the activation domain of SRF. RAP74 is the specific target for all transcriptions activated by SRF.

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