Title of article :
Molecular Structure of Human TFIIH
Author/Authors :
Patrick Schultz، نويسنده , , Sébastien Fribourg، نويسنده , , Arnaud Poterszman، نويسنده , , Véronique Mallouh، نويسنده , , Dino Moras، نويسنده , , Jean Marc Egly، نويسنده ,
Issue Information :
هفته نامه با شماره پیاپی سال 2000
Pages :
9
From page :
599
To page :
607
Abstract :
TFIIH is a multiprotein complex required for both transcription and DNA repair. Single particles of human TFIIH were revealed by electron microscopy and image processing at a resolution of 3.8 nm. TFIIH is 16 × 12.5 × 7.5 nm in size and is organized into a ring-like structure from which a large protein domain protrudes out. A subcomplex assembled from five recombinant core subunits also forms a circular architecture that can be superimposed on the ring found in human TFIIH. Immunolabeling experiments localize several subunits: p44, within the ring structure, forms the base of the protruding protein density which includes the cdk7 kinase, cyclin H, and MAT1. Within the ring structure, p44 was flanked on either side by the XPB and XPD helicases. These observations provide us with a quartenary organizational model of TFIIH.
Journal title :
CELL
Serial Year :
2000
Journal title :
CELL
Record number :
1017082
Link To Document :
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