Peter Weil
Faculty Member
Last active: 11/4/2015

Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIID.

Papai G, Tripathi MK, Ruhlmann C, Werten S, Crucifix C, Weil PA, Schultz P
Structure. 2009 17 (3): 363-73

PMID: 19278651 · PMCID: PMC2677412 · DOI:10.1016/j.str.2009.01.006

The general transcription factor TFIID is a large multisubunit complex required for the transcription of most protein-encoding genes by RNA polymerase II. Taking advantage of a TFIID preparation partially depleted in the initiator-binding Taf2p subunit, we determined the conformational and biochemical variations of the complex by electron tomography and cryo-electron microscopy of single molecules. Image analysis revealed the extent of conformational flexibility of the complex and the selection of the most homogeneous TFIID subpopulation allowed us to determine an improved structural model at 23 Angstroms resolution. This study also identified two subpopulations of Taf2p-containing and Taf2p-depleted TFIID molecules. By comparing these two TFIID species we could infer the position of Taf2p, which was confirmed by immunolabeling using a subunit-specific antibody. Mapping the position of this crucial subunit in the vicinity of Taf1p and of TBP sheds new light on its role in promoter recognition.

MeSH Terms (11)

Amino Acid Sequence Binding Sites Cryoelectron Microscopy Models, Molecular Molecular Sequence Data Protein Conformation Protein Subunits Saccharomyces cerevisiae Proteins Structure-Activity Relationship TATA-Binding Protein Associated Factors Transcription Factor TFIID

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