Fungal Transcription Factor Database
Detalied information of reference
Pubmed ID (PMID)
8855225
Paper type
Title
Elongation factor TFIIS contains three structural domains: solution structure of domain II.
Abstract
Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. Limited proteolytic digestion showed that yeast TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III) are required for transcription activity. The structure of domain III has been solved previously by using NMR spectroscopy. Here, we report the NMR-derived structure of domain II: a three-helix bundle built around a hydrophobic core composed largely of three tyrosines protruding from one face of the C-terminal helix. The arrangement of known inactivating mutations of TFIIS suggests that two surfaces of domain II are critical for transcription activity.
Authors
Morin PE, Awrey DE, Edwards AM, Arrowsmith CH.
Affiliation
Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.
Journal / Pages
Proceedings of the National Academy of Sciences of the United States of America., 1996 : 93(20), 10604~10608