Solution structure of a TBP-TAF(sub II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP

Article Abstract:

A study was conducted on the solution structure of the complex resulting from the dinging of the TATA box-binding protein (TBP) to the 230 KDa Drosophila TBP-associated factors (TAF (sub II)) negative terminal. Results showed that the TBP-binding surface of the 230 KDa Drosophila TAF (sub II) mimics the partially unwound TATA box's minor groove surface in the TBP-TATA complex. The protein mimicry provides the structural basis involve in the negative regulation of the TATA box-binding activity by the 230 KDa Drosophila TAF (sub II) within the transcription factor IID.

Protein binding, Drosophila, DNA binding proteins

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Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A

Article Abstract:

The regulation of the p300 and p300/CBP-associated factor (PCAF) histone acetyltransferases (HAT) was investigated. Results showed that the basic helix-loop-helix protein Twist directly binds two independent HAT domains and regulates the HAT activities of p300 and PCAF. It was also found that the N terminus of the Twist is the primary domain interacting with p300 and PCAF and that the effects of the Twist are imitated by the adenovirus E1A protein.

Proteins

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

Article Abstract:

The intrinsic histone acetyltransferase activity of the p300/CBP transcriptional adaptor is investigated. The p300/CBP acetylates all the four core histones in nucleosomes. Evidence indicates that p300/CBP, more than being a simple adaptor between DNA-binding factors and P/CAF or transcription factors, also directly influences transcriptional regulation through targeted acetylation of chromatin.

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