1vd4

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Solution structure of the zinc finger domain of TFIIE alpha

Overview

The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is, phylogenetically conserved and is essential for transcription. Here, we, determined the solution structure of this domain by using NMR. It, consisted of one alpha-helix and five beta-strands, showing novel features, distinct from previously determined zinc-binding structures. We created, point mutants of TFIIEalpha in this domain and examined their binding, abilities to other general transcription factors as well as their, transcription activities. Four Zn(2+)-ligand mutants, in which each of, cysteine residues at positions 129, 132, 154, and 157 was replaced by, alanine, possessed no transcription activities on a linearized template, whereas, on a supercoiled template, interesting functional asymmetry was, observed: although the C-terminal two mutants abolished transcription, activity (<5%), the N-terminal two mutants retained about 20% activities., The N-terminal two mutants bound stronger to the small subunit of TFIIF, than the wild type and the C-terminal two mutants were impaired in their, binding abilities to the XPB subunits of TFIIH. These suggest that the, structural integrity of the zinc finger domain is essential for the TFIIE, function, particularly in the transition from the transcription initiation, to elongation and the conformational tuning of this domain for appropriate, positioning of TFIIF, TFIIH, and polymerase II would be needed depending, on the situation and timing.

About this Structure

1VD4 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.

Reference

A novel zinc finger structure in the large subunit of human general transcription factor TFIIE., Okuda M, Tanaka A, Arai Y, Satoh M, Okamura H, Nagadoi A, Hanaoka F, Ohkuma Y, Nishimura Y, J Biol Chem. 2004 Dec 3;279(49):51395-403. Epub 2004 Sep 22. PMID:15385556

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