Structure of human TFIID and mechanism of TBP loading onto promoter DNA
Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E.
American Association for the Advancement of Science (AAAS)
Published 2018
American Association for the Advancement of Science (AAAS)
Published 2018
Publication Date: |
2018-12-21
|
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Publisher: |
American Association for the Advancement of Science (AAAS)
|
Print ISSN: |
0036-8075
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Electronic ISSN: |
1095-9203
|
Topics: |
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
|
Keywords: |
Biochemistry, Online Only
|
Published by: |
_version_ | 1836489295166177280 |
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autor | Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. |
beschreibung | The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. |
citation_standardnr | 6373480 |
datenlieferant | ipn_articles |
feed_id | 25 |
feed_publisher | American Association for the Advancement of Science (AAAS) |
feed_publisher_url | http://www.aaas.org/ |
insertion_date | 2018-12-21 |
journaleissn | 1095-9203 |
journalissn | 0036-8075 |
publikationsjahr_anzeige | 2018 |
publikationsjahr_facette | 2018 |
publikationsjahr_intervall | 7984:2015-2019 |
publikationsjahr_sort | 2018 |
publisher | American Association for the Advancement of Science (AAAS) |
quelle | Science |
relation | http://science.sciencemag.org/cgi/content/short/362/6421/eaau8872?rss=1 |
schlagwort | Biochemistry, Online Only |
search_space | articles |
shingle_author_1 | Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. |
shingle_author_2 | Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. |
shingle_author_3 | Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. |
shingle_author_4 | Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. |
shingle_catch_all_1 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA Biochemistry, Online Only The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_2 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA Biochemistry, Online Only The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_3 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA Biochemistry, Online Only The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_catch_all_4 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA Biochemistry, Online Only The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo–electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box–binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., Nogales, E. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
shingle_title_1 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
shingle_title_2 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
shingle_title_3 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
shingle_title_4 | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
timestamp | 2025-07-01T23:31:12.962Z |
titel | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
titel_suche | Structure of human TFIID and mechanism of TBP loading onto promoter DNA |
topic | W V TE-TZ SQ-SU WW-YZ TA-TD U |
uid | ipn_articles_6373480 |