Mapping histone fold TAFs within yeast TFIID

The transcription factor TFIID is a large multiprotein complex, composed of the TATA box‐binding protein (TBP) and 14 TBP‐associated factors (TAFs), which plays a key role in the regulation of gene expression by RNA polymerase II. The three‐dimensional structure of yeast (y) TFIID, determined at ∼3...

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Published in:The EMBO journal 2002-07, Vol.21 (13), p.3424-3433
Main Authors: Leurent, Claire, Sanders, Steven, Ruhlmann, Christine, Mallouh, Véronique, Weil, P.Anthony, Kirschner, Doris B., Tora, Laszlo, Schultz, Patrick
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
Biochemistry, Molecular Biology
Dimerization
Drosophila Proteins - chemistry
EMBO09
EMBO40
histone fold domains
Histones - chemistry
Human factors
Humans
Image Processing, Computer-Assisted
immunolabelling
Life Sciences
Macromolecular Substances
Microscopy, Electron
Microscopy, Immunoelectron
Models, Molecular
Multiprotein Complexes
Precipitin Tests
Protein Conformation
Protein Interaction Mapping
Protein Structure, Tertiary
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - ultrastructure
Species Specificity
Structure-Activity Relationship
three-dimensional model
transcription factor IID
Transcription Factor TFIID
Transcription Factors - chemistry
Transcription Factors - classification
Transcription Factors - ultrastructure
Transcription Factors, TFII - chemistry
Transcription Factors, TFII - ultrastructure
Yeasts
yTAFs
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container_end_page 3433
container_issue 13
container_start_page 3424
container_title The EMBO journal
container_volume 21
creator Leurent, Claire
Sanders, Steven
Ruhlmann, Christine
Mallouh, Véronique
Weil, P.Anthony
Kirschner, Doris B.
Tora, Laszlo
Schultz, Patrick
description The transcription factor TFIID is a large multiprotein complex, composed of the TATA box‐binding protein (TBP) and 14 TBP‐associated factors (TAFs), which plays a key role in the regulation of gene expression by RNA polymerase II. The three‐dimensional structure of yeast (y) TFIID, determined at ∼3 nm resolution by electron microscopy and image analysis, resembles a molecular clamp formed by three major lobes connected by thin linking domains. The yTFIID is structurally similar to the human factor although the clamp appears more closed in the yeast complex, probably reflecting the conformational flexibility of the structure. Immunolabelling experiments showed that nine TAFs that contain the histone fold structural motif were located in three distinct substructures of TFIID. The distribution of these TAFs showed that the previously reported pair‐wise interactions between histone fold domain (HFD)‐containing TAFs are likely to occur in the native yTFIID complex. Most of the HFD‐containing TAFs have been found in two distinct lobes, thus revealing an unexpected and novel molecular organization of TFIID.
doi_str_mv 10.1093/emboj/cdf342
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Most of the HFD‐containing TAFs have been found in two distinct lobes, thus revealing an unexpected and novel molecular organization of TFIID.</description><subject>Amino Acid Motifs</subject><subject>Animals</subject><subject>Biochemistry, Molecular Biology</subject><subject>Dimerization</subject><subject>Drosophila Proteins - chemistry</subject><subject>EMBO09</subject><subject>EMBO40</subject><subject>histone fold domains</subject><subject>Histones - chemistry</subject><subject>Human factors</subject><subject>Humans</subject><subject>Image Processing, Computer-Assisted</subject><subject>immunolabelling</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>Microscopy, Electron</subject><subject>Microscopy, Immunoelectron</subject><subject>Models, Molecular</subject><subject>Multiprotein Complexes</subject><subject>Precipitin Tests</subject><subject>Protein Conformation</subject><subject>Protein Interaction Mapping</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - ultrastructure</subject><subject>Species Specificity</subject><subject>Structure-Activity Relationship</subject><subject>three-dimensional model</subject><subject>transcription factor IID</subject><subject>Transcription Factor TFIID</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - classification</subject><subject>Transcription Factors - ultrastructure</subject><subject>Transcription Factors, TFII - chemistry</subject><subject>Transcription Factors, TFII - ultrastructure</subject><subject>Yeasts</subject><subject>yTAFs</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqFkt1v0zAUxS0EYmXwxiso4gEJaWG-_ojjBx7KWLeiDiRUBuLFcpqbNiVNip1s9L_HJVUZA8GTJft37jm6x4Q8BvoSqObHuMqa5fEsL7hgd8gAREJjRpW8SwaUJRALSPUBeeD9klIqUwX3yQGwoFSCD8jRhV2vy3oeLUrfNjVGRVPl0XQ48tF12S7KOtqg9W00HY3Hbx6Se4WtPD7anYfk4-h0enIeT96fjU-Gk3iWgKSxZEIiK3iSKJVrzDNbBF8lqM20SAtprciZxiLVimvEBKzSXAoBmKWAqPkhedXPXXfZCvMZ1q2zlVm7cmXdxjS2NL-_1OXCzJsrAyyhGoL-Ra9f3FKdDydme0cFSE45vdqyz3dervnWoW_NqvQzrCpbY9N5oyBVXISk_wMhFYxTEAF8dgtcNp2rw8IMaMkkSNjaHvXQzDXeOyz2OYGaba_mZ6-m7zXgT29u5Be8KzIAsgeuywo3_xxmTi9ev1VSC5nQoIt7nQ-Seo7uRti_B3nS87VtO4d7oz_mhe-E3_fP1n01ieJKmk_vzgz9fDm6ZNMv5gP_AdPq1pI</recordid><startdate>20020701</startdate><enddate>20020701</enddate><creator>Leurent, Claire</creator><creator>Sanders, Steven</creator><creator>Ruhlmann, Christine</creator><creator>Mallouh, Véronique</creator><creator>Weil, P.Anthony</creator><creator>Kirschner, Doris B.</creator><creator>Tora, Laszlo</creator><creator>Schultz, Patrick</creator><general>John Wiley &amp; 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subjects Amino Acid Motifs
Animals
Biochemistry, Molecular Biology
Dimerization
Drosophila Proteins - chemistry
EMBO09
EMBO40
histone fold domains
Histones - chemistry
Human factors
Humans
Image Processing, Computer-Assisted
immunolabelling
Life Sciences
Macromolecular Substances
Microscopy, Electron
Microscopy, Immunoelectron
Models, Molecular
Multiprotein Complexes
Precipitin Tests
Protein Conformation
Protein Interaction Mapping
Protein Structure, Tertiary
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - ultrastructure
Species Specificity
Structure-Activity Relationship
three-dimensional model
transcription factor IID
Transcription Factor TFIID
Transcription Factors - chemistry
Transcription Factors - classification
Transcription Factors - ultrastructure
Transcription Factors, TFII - chemistry
Transcription Factors, TFII - ultrastructure
Yeasts
yTAFs
title Mapping histone fold TAFs within yeast TFIID
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