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Comprehensive study of the ZAD family of zinc finger transcription factors in Drosophila melanogaster
- Date Issued:
- 2012
- Summary:
- The zinc finger associated domain (ZAD) family of transcription factors from Drosophila melanogaster is not well described in the literature, in part because it is very difficult to study by traditional mutagenesis screens. Bioinformatic studies indicate this is due to overlapping functions remaining after a recent evolutionary divergence. I set out to use in vitro-binding techniques to identify the characteristics of the ZAD family and test this theory. I have constructed glutathione S-transferase (GST)-ZAD domain chimeric proteins for use in pull down protein binding assays,and GST-Zinc finger (ZnF) array domain chimera for electrophoretic mobility shift assays (EMSA). Protein binding assays indicated two putative conserved interactors, similar to the analogous KRAB system in mammals. ... Competitive bindings were carried out to show a specificity of binding conferred by the identified conserved positions. While the consensus binding sites show relatively few similarities, the predicted target genes identified by the consensus binding sites show significant overlap. The nature of this overlap conforms to the known characteristics of the ZAD family but points to a more positive selection to maintain conservation of function.
Title: | Comprehensive study of the ZAD family of zinc finger transcription factors in Drosophila melanogaster. |
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Name(s): |
Krystel, Joseph. Charles E. Schmidt College of Science Department of Biological Sciences |
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Type of Resource: | text | |
Genre: | Electronic Thesis Or Dissertation | |
Date Issued: | 2012 | |
Publisher: | Florida Atlantic University | |
Physical Form: | electronic | |
Extent: | xii, 117 p. : ill. (some col.) | |
Language(s): | English | |
Summary: | The zinc finger associated domain (ZAD) family of transcription factors from Drosophila melanogaster is not well described in the literature, in part because it is very difficult to study by traditional mutagenesis screens. Bioinformatic studies indicate this is due to overlapping functions remaining after a recent evolutionary divergence. I set out to use in vitro-binding techniques to identify the characteristics of the ZAD family and test this theory. I have constructed glutathione S-transferase (GST)-ZAD domain chimeric proteins for use in pull down protein binding assays,and GST-Zinc finger (ZnF) array domain chimera for electrophoretic mobility shift assays (EMSA). Protein binding assays indicated two putative conserved interactors, similar to the analogous KRAB system in mammals. ... Competitive bindings were carried out to show a specificity of binding conferred by the identified conserved positions. While the consensus binding sites show relatively few similarities, the predicted target genes identified by the consensus binding sites show significant overlap. The nature of this overlap conforms to the known characteristics of the ZAD family but points to a more positive selection to maintain conservation of function. | |
Identifier: | 820360044 (oclc), 3355627 (digitool), FADT3355627 (IID), fau:3953 (fedora) | |
Note(s): |
by Joseph Krystel. Thesis (Ph.D.)--Florida Atlantic University, 2012. Includes bibliography. Mode of access: World Wide Web. System requirements: Adobe Reader. |
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Subject(s): |
Cellular signal transduction Drosophila melanogaster -- Cytogenetics Transcription factors Zinc-finger proteins -- Synthesis Genetic transcription -- Regulation Gene expression |
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Persistent Link to This Record: | http://purl.flvc.org/FAU/3355627 | |
Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
Host Institution: | FAU |