Structure of human TFIID and mechanism of TBP loading onto promoter DNA

Publication Date:
2018-12-21
Publisher:
American Association for the Advancement of Science (AAAS)
Print ISSN:
0036-8075
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
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