A histone fold TAF octamer within the yeast TFIID transcriptional coactivator

William Selleck; Ryan Howley; Qiaojun Fang; Vladimir Podolny; Michael G. Fried; Stephen Buratowski; Song Tan

doi:10.1038/90408

A histone fold TAF octamer within the yeast TFIID transcriptional coactivator

William Selleck, Ryan Howley, Qiaojun Fang, Vladimir Podolny, Michael G. Fried, Stephen Buratowski, Song Tan

Research output: Contribution to journal › Article › peer-review

62 Scopus citations

Abstract

Gene activity in a eukaryotic cell is regulated by accessory factors to RNA polymerase II, which include the general transcription factor complex TFIID, composed of TBP and TBP-associated factors (TAFs). Three TAFs that contain histone fold motifs (yTAF17, yTAF60 and yTAF61) are critical for transcriptional regulation in the yeast Saccharomyces cerevisiae and are found in both TFIID and SAGA, a multicomponent histone acetyltransferase transcriptional coactivator. Although these three TAFs were proposed to assemble into a pseudooctamer complex, we find instead that yTAF17, yTAF60 and yTAF61 form a specific TAF octamer complex with a fourth TAF found in TFIID, yTAF48. We have reconstituted this complex in vitro and established that it is an octamer containing two copies each of the four components. Point mutations within the histone folds disrupt the octamer in vitro, and temperature-sensitive mutations in the histone folds can be specifically suppressed by overexpressing the other TAF octamer components in vivo. Our results indicate that the TAF octamer is similar both in stoichiometry and histone fold interactions to the histone octamer component of chromatin.

Original language	English
Pages (from-to)	695-700
Number of pages	6
Journal	Nature Structural Biology
Volume	8
Issue number	8
DOIs	https://doi.org/10.1038/90408
State	Published - 2001

Bibliographical note

Funding Information:
We thank B. Schlansky and M. Song for technical assistance; C. Brown, J. Reese, B. Simpson and J. Workman for critical reading of the manuscript, and to the gene regulation community at Penn State for stimulating discussions. We are also grateful to T. Richmond, in whose laboratory preliminary studies for this project were initiated. This work was supported by NIH grants to M.F., S.B. and S.T. S.B. is a Leukemia and Lymphoma Society Scholar.

Funding

We thank B. Schlansky and M. Song for technical assistance; C. Brown, J. Reese, B. Simpson and J. Workman for critical reading of the manuscript, and to the gene regulation community at Penn State for stimulating discussions. We are also grateful to T. Richmond, in whose laboratory preliminary studies for this project were initiated. This work was supported by NIH grants to M.F., S.B. and S.T. S.B. is a Leukemia and Lymphoma Society Scholar.

Funders	Funder number
National Institutes of Health (NIH)

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "A histone fold TAF octamer within the yeast TFIID transcriptional coactivator",

abstract = "Gene activity in a eukaryotic cell is regulated by accessory factors to RNA polymerase II, which include the general transcription factor complex TFIID, composed of TBP and TBP-associated factors (TAFs). Three TAFs that contain histone fold motifs (yTAF17, yTAF60 and yTAF61) are critical for transcriptional regulation in the yeast Saccharomyces cerevisiae and are found in both TFIID and SAGA, a multicomponent histone acetyltransferase transcriptional coactivator. Although these three TAFs were proposed to assemble into a pseudooctamer complex, we find instead that yTAF17, yTAF60 and yTAF61 form a specific TAF octamer complex with a fourth TAF found in TFIID, yTAF48. We have reconstituted this complex in vitro and established that it is an octamer containing two copies each of the four components. Point mutations within the histone folds disrupt the octamer in vitro, and temperature-sensitive mutations in the histone folds can be specifically suppressed by overexpressing the other TAF octamer components in vivo. Our results indicate that the TAF octamer is similar both in stoichiometry and histone fold interactions to the histone octamer component of chromatin.",

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AU - Howley, Ryan

AU - Fang, Qiaojun

AU - Podolny, Vladimir

AU - Fried, Michael G.

AU - Buratowski, Stephen

AU - Tan, Song

N1 - Funding Information: We thank B. Schlansky and M. Song for technical assistance; C. Brown, J. Reese, B. Simpson and J. Workman for critical reading of the manuscript, and to the gene regulation community at Penn State for stimulating discussions. We are also grateful to T. Richmond, in whose laboratory preliminary studies for this project were initiated. This work was supported by NIH grants to M.F., S.B. and S.T. S.B. is a Leukemia and Lymphoma Society Scholar.

PY - 2001

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N2 - Gene activity in a eukaryotic cell is regulated by accessory factors to RNA polymerase II, which include the general transcription factor complex TFIID, composed of TBP and TBP-associated factors (TAFs). Three TAFs that contain histone fold motifs (yTAF17, yTAF60 and yTAF61) are critical for transcriptional regulation in the yeast Saccharomyces cerevisiae and are found in both TFIID and SAGA, a multicomponent histone acetyltransferase transcriptional coactivator. Although these three TAFs were proposed to assemble into a pseudooctamer complex, we find instead that yTAF17, yTAF60 and yTAF61 form a specific TAF octamer complex with a fourth TAF found in TFIID, yTAF48. We have reconstituted this complex in vitro and established that it is an octamer containing two copies each of the four components. Point mutations within the histone folds disrupt the octamer in vitro, and temperature-sensitive mutations in the histone folds can be specifically suppressed by overexpressing the other TAF octamer components in vivo. Our results indicate that the TAF octamer is similar both in stoichiometry and histone fold interactions to the histone octamer component of chromatin.

AB - Gene activity in a eukaryotic cell is regulated by accessory factors to RNA polymerase II, which include the general transcription factor complex TFIID, composed of TBP and TBP-associated factors (TAFs). Three TAFs that contain histone fold motifs (yTAF17, yTAF60 and yTAF61) are critical for transcriptional regulation in the yeast Saccharomyces cerevisiae and are found in both TFIID and SAGA, a multicomponent histone acetyltransferase transcriptional coactivator. Although these three TAFs were proposed to assemble into a pseudooctamer complex, we find instead that yTAF17, yTAF60 and yTAF61 form a specific TAF octamer complex with a fourth TAF found in TFIID, yTAF48. We have reconstituted this complex in vitro and established that it is an octamer containing two copies each of the four components. Point mutations within the histone folds disrupt the octamer in vitro, and temperature-sensitive mutations in the histone folds can be specifically suppressed by overexpressing the other TAF octamer components in vivo. Our results indicate that the TAF octamer is similar both in stoichiometry and histone fold interactions to the histone octamer component of chromatin.

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A histone fold TAF octamer within the yeast TFIID transcriptional coactivator

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