The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-08

AUTHORS

Hung-Ta Chen, Linda Warfield, Steven Hahn

ABSTRACT

We incorporated the non-natural photoreactive amino acid p-benzoyl-L-phenylalanine (Bpa) into the RNA polymerase II (Pol II) surface surrounding the central cleft formed by the Rpb1 and Rpb2 subunits. Photo-cross-linking of preinitiation complexes (PICs) with these Pol II derivatives and hydroxyl-radical cleavage assays revealed that the TFIIF dimerization domain interacts with the Rpb2 lobe and protrusion domains adjacent to Rpb9, while TFIIE cross-links to the Rpb1 clamp domain on the opposite side of the Pol II central cleft. Mutations in the Rpb2 lobe and protrusion domains alter both Pol II-TFIIF binding and the transcription start site, a phenotype associated with mutations in TFIIF, Rpb9 and TFIIB. Together with previous biochemical and structural studies, these findings illuminate the structural organization of the PIC and the network of protein-protein interactions involved in transcription start site selection. More... »

PAGES

696-703

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb1272

DOI

http://dx.doi.org/10.1038/nsmb1272

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048916764

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17632521


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