The histone fold is a key structural motif of transcription factor TFIID

Citation
Yg. Gangloff et al., The histone fold is a key structural motif of transcription factor TFIID, TRENDS BIOC, 26(4), 2001, pp. 250-257
Citations number
50
Categorie Soggetti
Biochemistry & Biophysics
Journal title
TRENDS IN BIOCHEMICAL SCIENCES
ISSN journal
09680004 → ACNP
Volume
26
Issue
4
Year of publication
2001
Pages
250 - 257
Database
ISI
SICI code
0968-0004(200104)26:4<250:THFIAK>2.0.ZU;2-V
Abstract
Transcription factor TFIID is a multiprotein complex composed of the TATA b inding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit co mposition of this factor is highly conserved from yeast to mammals. X-ray c rystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide ins ights into the overall organization of this complex.