title: Molecular structure of human TFIIH.
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 x 12.5 x 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.
authors.affiliation: Institut de Génétique et de Biologie Moléclaire et Cellulaire, CNRS/INSERM/ULP, Illkirch, France. pat@moorea.u-strasbg.fr
authors.forename: P
authors.initials: P
authors.lastname: Schultz
authors.forename: S
authors.initials: S
authors.lastname: Fribourg
authors.forename: A
authors.initials: A
authors.lastname: Poterszman
authors.forename: V
authors.initials: V
authors.lastname: Mallouh
authors.forename: D
authors.initials: D
authors.lastname: Moras
authors.forename: J M
authors.initials: JM
authors.lastname: Egly
mesh_terms: D000911:Antibodies, Monoclonal; D056748:Cyclin H; D018844:Cyclin-Dependent Kinases; D016213:Cyclins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D006367:HeLa Cells; D006801:Humans; D007091:Image Processing, Computer-Assisted; D046911:Macromolecular Substances; D016253:Microscopy, Immunoelectron; D008958:Models, Molecular; D046912:Multiprotein Complexes; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D012333:RNA, Messenger / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D051758:Transcription Factor TFIIH; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D019473:Transcription Factors, TFII; D014158:Transcription, Genetic; D051759:Xeroderma Pigmentosum Group D Protein; D000095043:Cyclin-Dependent Kinase-Activating Kinase
chemical_list: D000911:Antibodies, Monoclonal; C534751:CCNH protein, human; D056748:Cyclin H; D016213:Cyclins; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D046912:Multiprotein Complexes; D011506:Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D014157:Transcription Factors; D019473:Transcription Factors, TFII; C072022:XPBC-ERCC-3 protein; D051758:Transcription Factor TFIIH; D017346:Protein Serine-Threonine Kinases; D018844:Cyclin-Dependent Kinases; D004265:DNA Helicases; D051759:Xeroderma Pigmentosum Group D Protein; C497292:ERCC2 protein, human; D000095043:Cyclin-Dependent Kinase-Activating Kinase; C000722416:CDK7 protein, human