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The doublesex transcription factor: ...

Bayrer, James Robert.

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The doublesex transcription factor: Structural and functional studies of a sex-determining factor.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The doublesex transcription factor: Structural and functional studies of a sex-determining factor./
作者:	Bayrer, James Robert.
面頁冊數:	338 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-10, Section: B, page: 5375.
Contained By:	Dissertation Abstracts International66-10B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3193525
ISBN:	9780542367694

The doublesex transcription factor: Structural and functional studies of a sex-determining factor.
Bayrer, James Robert.

The doublesex transcription factor: Structural and functional studies of a sex-determining factor. - 338 p.

Source: Dissertation Abstracts International, Volume: 66-10, Section: B, page: 5375.

Thesis (Ph.D.)--Case Western Reserve University, 2006.

Doublesex (DSX) is a transcription factor responsible for the regulation of sexual differentiation in Drosophila. Alternate splicing gives rise to male- and female-specific isoforms. A potent modulator of the yolk protein gene (yp), the male isoform (DSX M) represses transcription of yp whereas the female isoform (DSXF) is an activator. DSX contains two recognized domains, an N-terminal DNA-binding domain (shared between isoforms) and a C-terminal domain (CTD) that is responsible for oligomerization and presumably transcriptional regulation. The CTDs contain sex-specific C-terminal sequences with opposite gene-regulatory properties. We have solved the crystal structure of the core CTD dimerization domain to a resolution of 1.6 A using s&barbelow;ingle-wavelength a&barbelow;nomalous d&barbelow;ispersion (SAD) phasing. The crystal structure reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. To our knowledge this is its first report in a transcription factor, and the first structure of a dimeric UBA domain. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative Ub-binding surface. The unexpected observation of a UBA fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors.

ISBN: 9780542367694Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

The doublesex transcription factor: Structural and functional studies of a sex-determining factor.
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500 $a Adviser: Michael A. Weiss.
502 $a Thesis (Ph.D.)--Case Western Reserve University, 2006.
520 $a Doublesex (DSX) is a transcription factor responsible for the regulation of sexual differentiation in Drosophila. Alternate splicing gives rise to male- and female-specific isoforms. A potent modulator of the yolk protein gene (yp), the male isoform (DSX M) represses transcription of yp whereas the female isoform (DSXF) is an activator. DSX contains two recognized domains, an N-terminal DNA-binding domain (shared between isoforms) and a C-terminal domain (CTD) that is responsible for oligomerization and presumably transcriptional regulation. The CTDs contain sex-specific C-terminal sequences with opposite gene-regulatory properties. We have solved the crystal structure of the core CTD dimerization domain to a resolution of 1.6 A using s&barbelow;ingle-wavelength a&barbelow;nomalous d&barbelow;ispersion (SAD) phasing. The crystal structure reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. To our knowledge this is its first report in a transcription factor, and the first structure of a dimeric UBA domain. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative Ub-binding surface. The unexpected observation of a UBA fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors.
520 $a Intersexual development of XX Drosophila (karyotypic females) is associated with mutation G398D, encoded in female-specific exon 4. G398 lies within CTD. We demonstrate that the intersexual mutation blocks dimerization leading to non-native aggregation. Analysis of diverse substitutions at 398 indicates that only alanine (found in the male isoform) is tolerated. The structure of the dimer suggests that side chains larger than alanine would clash at the interface; dimerization of the G398D variant would be further destabilized by an uncompensated buried charge. The instability of the variant monomer suggests that folding and dimerization are coupled. Such coupling---although a general feature of leucine zippers and other helical dimerization elements---is novel among UBA domains. We extend these studies by hydrogen exchange analysis, demonstrating long-lived resonances in the dimer interface. We further present evidence for ubiquitin-binding by CTDF, suggesting a previously unappreciated role for ubiquitin in sex determination. Our results define a new role for the UBA fold in transcription and rationalize the impaired sexual differentiation of a model organism.
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650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
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710 2 0 $a Case Western Reserve University. $3 1017714
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