東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Protein interactions of partner of p...

Das, Tirtha Kamal.

Linked to FindBook

Google Book

Amazon

博客來

Protein interactions of partner of paired and its vertebrate homologs.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Protein interactions of partner of paired and its vertebrate homologs./
Author:	Das, Tirtha Kamal.
Description:	161 p.
Notes:	Source: Dissertation Abstracts International, Volume: 62-02, Section: B, page: 0663.
Contained By:	Dissertation Abstracts International62-02B.
Subject:	Biology, Genetics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3005640
ISBN:	0493145966

Protein interactions of partner of paired and its vertebrate homologs.
Das, Tirtha Kamal.

Protein interactions of partner of paired and its vertebrate homologs. - 161 p.

Source: Dissertation Abstracts International, Volume: 62-02, Section: B, page: 0663.

Thesis (Ph.D.)--Wesleyan University, 2001.

Patterning of the undifferentiated Drosophila embryo relies on a hierarchical cascade of segmentation gene products. My work focused on understanding the role of the pair-rule segmentation gene <italic>paired</italic> (<italic> prd</italic>) in this hierarchical process of gene activation. The Prd protein is a transcription factor that plays a key role in activating downstream segmentation genes like <italic>engrailed</italic> (<italic>en</italic>), <italic>gooseberry </italic> (<italic>gsb</italic>), and <italic>wingless</italic> (<italic> wg</italic>). Activation of these downstream genes is crucial for creating the early subdivisions of the undifferentiated embryo, which eventually gives rise to a normal adult fly. I have undertaken various strategies to carefully dissect the role of <italic>prd</italic> during this segmentation process.

ISBN: 0493145966Subjects--Topical Terms:

1017730
Biology, Genetics.

Protein interactions of partner of paired and its vertebrate homologs.
LDR:03767nmm 2200313 4500 001 1810427
005 20040311140854.5
008 130610s2001 eng d
020 $a 0493145966
035 $a (UnM)AAI3005640
035 $a AAI3005640
040 $a UnM $c UnM
100 1 $a Das, Tirtha Kamal. $3 1900039
245 1 0 $a Protein interactions of partner of paired and its vertebrate homologs.
300 $a 161 p.
500 $a Source: Dissertation Abstracts International, Volume: 62-02, Section: B, page: 0663.
500 $a Adviser: Michael P. Weir.
502 $a Thesis (Ph.D.)--Wesleyan University, 2001.
520 $a Patterning of the undifferentiated Drosophila embryo relies on a hierarchical cascade of segmentation gene products. My work focused on understanding the role of the pair-rule segmentation gene <italic>paired</italic> (<italic> prd</italic>) in this hierarchical process of gene activation. The Prd protein is a transcription factor that plays a key role in activating downstream segmentation genes like <italic>engrailed</italic> (<italic>en</italic>), <italic>gooseberry </italic> (<italic>gsb</italic>), and <italic>wingless</italic> (<italic> wg</italic>). Activation of these downstream genes is crucial for creating the early subdivisions of the undifferentiated embryo, which eventually gives rise to a normal adult fly. I have undertaken various strategies to carefully dissect the role of <italic>prd</italic> during this segmentation process.
520 $a The second chapter of my thesis outlines my analysis of the activation domain of the Prd protein. My analysis has shown that two <italic>prd</italic> transgenes can complement each other and activate downstream targets in embryos, if at least one transgene has an intact activation domain. My analysis has also shown that substituting the proline-rich activation domain of Prd with the glutamine rich activation domain of transcription factor SP1 prevents the Prd-SP1<sub>AD</sub> chimera from activating targets in embryos.
520 $a The third chapter of my thesis presents genetic analysis, performed in collaboration with other members in the Weir laboratory, to investigate the effects of P-element insertions in the vicinity of putative Prd protein interactors. These genetic analyses show that the P-element insertions do not affect the ability of Prd to activate downstream target genes, thereby suggesting that genes disrupted by these insertions do not work alongside Prd in the segmentation cascade.
520 $a The fourth chapter presents my analysis of protein interactions of Ppa, an F-box protein, and its vertebrate homologs. Previous work from our laboratory has shown that Ppa protein controls the stability of the Prd protein. My work has shown that Ppa controls Prd protein stability by targeting it to an SCF complex for degradation. I have identified vertebrate homologs of Ppa to start analyzing the role of Ppa in these organisms. My protein interaction studies have shown that vertebrate Ppa can associate with components of the SCF machinery, and have also provided preliminary evidence that vertebrate Ppa might interact with Pax3, the vertebrate equivalent of Drosophila Prd. Finally, my in situ hybridization studies have shown that <italic>ppa</italic> homologs in zebrafish might be expressed in regions of the embryo where Pax3 is also present. I postulate that a similar mechanism controls the stability of the Pax transcription factor Prd in Drosophila, and Pax3 in vertebrates.
590 $a School code: 0255.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Cell. $3 1017686
690 $a 0369
690 $a 0379
710 2 0 $a Wesleyan University. $3 1058128
773 0 $t Dissertation Abstracts International $g 62-02B.
790 1 0 $a Weir, Michael P., $e advisor
790 $a 0255
791 $a Ph.D.
792 $a 2001
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3005640