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Transcriptional repression mediated ...

Struffi, Paolo.

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Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3./
作者:	Struffi, Paolo.
面頁冊數:	205 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1665.
Contained By:	Dissertation Abstracts International65-04B.
標題:	Biology, Genetics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3129545
ISBN:	0496768042

Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3.
Struffi, Paolo.

Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3. - 205 p.

Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1665.

Thesis (Ph.D.)--Michigan State University, 2004.

The Drosophila Knirps protein is a short-range transcriptional repressor essential for proper embryonic development. Short-range repressors work over distances of less than 100--150 base pairs to inhibit activators in a local fashion, allowing multiple enhancers to be regulated autonomously. The mechanisms of short-range repression remain poorly understood at the molecular level. Knirps mediates repression in part by recruiting the co-repressor CtBP, but it also posses a CtBP-independent repression activity that maps to the N-terminus of the protein. The functional relevance of multiple repression activities is not well understood, but the findings that Knirps does not repress some cis-regulatory elements in the absence of CtBP, suggested that the co-factor may supply a unique function essential to repress certain types of activators. I assayed the CtBP-dependent and -independent repression activities of Knirps in Drosophila embryos and found that the requirement for CtBP at certain enhancers appears to reflect the need for overall higher levels of repression, rather than a requirement for an activity unique to CtBP. Thus, CtBP contributes quantitatively, rather than qualitatively to Knirps function.

ISBN: 0496768042Subjects--Topical Terms:

1017730
Biology, Genetics.

Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3.
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245 1 0 $a Transcriptional repression mediated by the Drosophila Knirps protein: Contributions of CtBP and Rpd3.
300 $a 205 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1665.
500 $a Adviser: David N. Arnosti.
502 $a Thesis (Ph.D.)--Michigan State University, 2004.
520 $a The Drosophila Knirps protein is a short-range transcriptional repressor essential for proper embryonic development. Short-range repressors work over distances of less than 100--150 base pairs to inhibit activators in a local fashion, allowing multiple enhancers to be regulated autonomously. The mechanisms of short-range repression remain poorly understood at the molecular level. Knirps mediates repression in part by recruiting the co-repressor CtBP, but it also posses a CtBP-independent repression activity that maps to the N-terminus of the protein. The functional relevance of multiple repression activities is not well understood, but the findings that Knirps does not repress some cis-regulatory elements in the absence of CtBP, suggested that the co-factor may supply a unique function essential to repress certain types of activators. I assayed the CtBP-dependent and -independent repression activities of Knirps in Drosophila embryos and found that the requirement for CtBP at certain enhancers appears to reflect the need for overall higher levels of repression, rather than a requirement for an activity unique to CtBP. Thus, CtBP contributes quantitatively, rather than qualitatively to Knirps function.
520 $a To investigate whether Knirps interacts with other co-factor/s in addition to CtBP, I generated transgenic flies that express inducible, double-tagged versions of Knirps and performed affinity purification experiments. Recombinant, full-length Knirps could be expressed in embryos at the same time as the endogenous factor and the protein acted as a functional repressor. Gel filtration chromatography of embryonic extracts expressing full-length Knirps indicate that the recombinant protein is part of a complex of &sim;450 kDa, suggesting that other factors in addition to CtBP interact with Knirps. In a survey of possible cofactors, we found that the histone deacetylase Rpd3 (HDACI) coimmunoprecipitates with Knirps and the two proteins cofractionate during gel filtration. To facilitate characterization of novel Knirps-interacting proteins, we developed a tandem affinity chromatography protocol from embryonic extracts overexpressing Knirps and find that Rpd3 copurifies with full-length Knirps, but not the CtBP-independent repression domain. To test the functional relevance of this association, we carried out dosage interaction assays, and find that the rpd3 and knirps interact genetically. Altogether these results suggest that histone deacetylation plays a role in short-range transcriptional repression mediated by Knirps.
590 $a School code: 0128.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
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690 $a 0307
710 2 0 $a Michigan State University. $3 676168
773 0 $t Dissertation Abstracts International $g 65-04B.
790 1 0 $a Arnosti, David N., $e advisor
790 $a 0128
791 $a Ph.D.
792 $a 2004
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