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In vivo role of TAF4 in TFIID struct...

Wright, Kevin James.

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In vivo role of TAF4 in TFIID structural integrity and co-activator function.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	In vivo role of TAF4 in TFIID structural integrity and co-activator function./
Author:	Wright, Kevin James.
Description:	122 p.
Notes:	Advisers: Robert Tijan; Michael Levine.
Contained By:	Dissertation Abstracts International68-08B.
Subject:	Biology, Genetics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3275657
ISBN:	9780549171362

In vivo role of TAF4 in TFIID structural integrity and co-activator function.
Wright, Kevin James.

In vivo role of TAF4 in TFIID structural integrity and co-activator function. - 122 p.

Advisers: Robert Tijan; Michael Levine.

Thesis (Ph.D.)--University of California, Berkeley, 2007.

Accurate, tightly regulated transcription is essential to the development and homeostasis of all organisms. In eukaryotes, this process requires the exquisitely choreographed cooperation between hundreds of polypeptides that relay signals to activate the gene, prepare the surrounding chromatin, recognize the gene promoter, and finally synthesize the encoded mRNA molecule. While most of the proteins or multi-protein complexes responsible for each of these steps have been identified over the last 30 years, the precise complex is made up of approximately 12 unique subunits. How each of these subunits contributes to TFIID structure and function has been a challenging problem that remains poorly understood. In this thesis I describe an in vivo analysis of TFIID architecture using RNA interference in Drosophila tissue culture cells. By systematically depleting individual subunits and monitoring the integrity of the complex I have identified a novel stable core sub-complex of TFIID comprising TAF4, TAF5, TAF6, TAF9, and TAF12. This unexpected finding revealed a structure and likely assembly pathway that is significantly different from what has been previously reported, and uncovered a number of novel aspects. For example, I describe a C-terminal region of TAF4 that is sufficient to nucleate a functional holo-TFIID complex, and also an N-terminal region of TAF6 sufficient for TFIID stability. Based on these data I present an updated model of TFIID assembly whereby the C-terminus of TAF4 and the N-terminus of TAF6 nucleate a stable core sub-complex that likely serves as a platform upon which TFIID-specific peripheral subunits TBP, TAF1, TAF2, and TAF11 are loaded.

ISBN: 9780549171362Subjects--Topical Terms:

1017730
Biology, Genetics.

In vivo role of TAF4 in TFIID structural integrity and co-activator function.
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020 $a 9780549171362
035 $a (UMI)AAI3275657
035 $a AAI3275657
040 $a UMI $c UMI
100 1 $a Wright, Kevin James. $3 1285806
245 1 0 $a In vivo role of TAF4 in TFIID structural integrity and co-activator function.
300 $a 122 p.
500 $a Advisers: Robert Tijan; Michael Levine.
500 $a Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 5220.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2007.
520 $a Accurate, tightly regulated transcription is essential to the development and homeostasis of all organisms. In eukaryotes, this process requires the exquisitely choreographed cooperation between hundreds of polypeptides that relay signals to activate the gene, prepare the surrounding chromatin, recognize the gene promoter, and finally synthesize the encoded mRNA molecule. While most of the proteins or multi-protein complexes responsible for each of these steps have been identified over the last 30 years, the precise complex is made up of approximately 12 unique subunits. How each of these subunits contributes to TFIID structure and function has been a challenging problem that remains poorly understood. In this thesis I describe an in vivo analysis of TFIID architecture using RNA interference in Drosophila tissue culture cells. By systematically depleting individual subunits and monitoring the integrity of the complex I have identified a novel stable core sub-complex of TFIID comprising TAF4, TAF5, TAF6, TAF9, and TAF12. This unexpected finding revealed a structure and likely assembly pathway that is significantly different from what has been previously reported, and uncovered a number of novel aspects. For example, I describe a C-terminal region of TAF4 that is sufficient to nucleate a functional holo-TFIID complex, and also an N-terminal region of TAF6 sufficient for TFIID stability. Based on these data I present an updated model of TFIID assembly whereby the C-terminus of TAF4 and the N-terminus of TAF6 nucleate a stable core sub-complex that likely serves as a platform upon which TFIID-specific peripheral subunits TBP, TAF1, TAF2, and TAF11 are loaded.
520 $a Using information gained from my analysis of TFIID stability, I next began to functionally characterize individual subunits within the complex by first identifying a bona fide target gene of the developmentally relevant Wingless signaling pathway in Drosophila that requires TFIID activity. Then, by developing a novel approach utilizing RNAi combined with overexpression to replace individual TFIID subunits with mutant forms, I show that the N-terminal co-activation domain of TAF4 is essential for the activation of the Wingless target gene naked cuticle. My results indicate a central role for TAF4 not only in the stable assembly of the core TFIID complex, but also in translating developmental signals into specific changes in gene expression profiles.
590 $a School code: 0028.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0307
690 $a 0369
690 $a 0487
710 2 $a University of California, Berkeley. $3 687832
773 0 $t Dissertation Abstracts International $g 68-08B.
790 $a 0028
790 1 0 $a Levine, Michael, $e advisor
790 1 0 $a Tijan, Robert, $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3275657