Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities.
The transcription/DNA repair factor TFIIH may be resolved into at least two subcomplexes: the core TFIIH and the cdk-activating kinase (CAK) complex. The CAK complex, which is also found free in the cell, is composed of cdk7, cyclin H, and MAT1. In the present work, we found that the C terminus of M...
Main Authors: | , , , , , |
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Format: | Journal article |
Language: | English |
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2000
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author | Busso, D Keriel, A Sandrock, B Poterszman, A Gileadi, O Egly, J |
author_facet | Busso, D Keriel, A Sandrock, B Poterszman, A Gileadi, O Egly, J |
author_sort | Busso, D |
collection | OXFORD |
description | The transcription/DNA repair factor TFIIH may be resolved into at least two subcomplexes: the core TFIIH and the cdk-activating kinase (CAK) complex. The CAK complex, which is also found free in the cell, is composed of cdk7, cyclin H, and MAT1. In the present work, we found that the C terminus of MAT1 binds to the cdk7 x cyclin H complex and activates the cdk7 kinase activity. The median portion of MAT1, which contains a coiled-coil motif, allows the binding of CAK to the TFIIH core through interactions with both XPD and XPB helicases. Furthermore, using recombinant TFIIH complexes, it is demonstrated that the N-terminal RING finger domain of MAT1 is crucial for transcription activation and participates to the phosphorylation of the C-terminal domain of the largest subunit of the RNA polymerase II. |
first_indexed | 2024-03-06T22:55:12Z |
format | Journal article |
id | oxford-uuid:60235d23-92db-4d3b-826a-5936100aabb8 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T22:55:12Z |
publishDate | 2000 |
record_format | dspace |
spelling | oxford-uuid:60235d23-92db-4d3b-826a-5936100aabb82022-03-26T17:51:30ZDistinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:60235d23-92db-4d3b-826a-5936100aabb8EnglishSymplectic Elements at Oxford2000Busso, DKeriel, ASandrock, BPoterszman, AGileadi, OEgly, JThe transcription/DNA repair factor TFIIH may be resolved into at least two subcomplexes: the core TFIIH and the cdk-activating kinase (CAK) complex. The CAK complex, which is also found free in the cell, is composed of cdk7, cyclin H, and MAT1. In the present work, we found that the C terminus of MAT1 binds to the cdk7 x cyclin H complex and activates the cdk7 kinase activity. The median portion of MAT1, which contains a coiled-coil motif, allows the binding of CAK to the TFIIH core through interactions with both XPD and XPB helicases. Furthermore, using recombinant TFIIH complexes, it is demonstrated that the N-terminal RING finger domain of MAT1 is crucial for transcription activation and participates to the phosphorylation of the C-terminal domain of the largest subunit of the RNA polymerase II. |
spellingShingle | Busso, D Keriel, A Sandrock, B Poterszman, A Gileadi, O Egly, J Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title | Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title_full | Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title_fullStr | Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title_full_unstemmed | Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title_short | Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities. |
title_sort | distinct regions of mat1 regulate cdk7 kinase and tfiih transcription activities |
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