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UBC Theses and Dissertations
Characterization of the S. cerevisiae Rap1 DNA binding domain and biochemical analysis of its interactions with telomeric and silencer DNA Stone, Geoffrey
Abstract
groove. Deletion of this region resulted in a protein able to bind telomere and silencer DNA with high affinity, suggesting that this region is not essential for DNA binding or HTH1-HTH2 cooperative interaction. Deletion of a "loop" region between HTH1 and HTH2 was also performed, and results suggested a role for this region in optimal binding of Rap 1 to tandemly repeated telomere sequences. Rapl is a multifunctional protein in S. cerevisiae. It plays a role in chromatin organization, gene silencing and transcriptional activation. Activation alone takes place using up to 100 Rapl DNA binding sites on the genome. All of these functions are mediated by Rapl binding to the DNA duplex, and the Rapl DBD structure must be adaptive to the requirements of the various cellular processes. This thesis suggests that the HTH1, HTH2, "tail" and "loop" regions are specifically designed to optimize Rapl function. Cooperative binding to DNA by HTH1-HTH2 allows a certain degree of degeneracy at high affinity binding sites. "Tail" interactions, while not essential for DNA binding, maintain binding site specificity at a "core" ACC sequence. Finally, the "loop" region allows proper alignment of HTH1 and HTH2, increasing the cooperative association of these two motifs.
Item Metadata
Title |
Characterization of the S. cerevisiae Rap1 DNA binding domain and biochemical analysis of its interactions with telomeric and silencer DNA
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
2000
|
Description |
groove. Deletion of this region resulted in a protein able to bind telomere and silencer DNA
with high affinity, suggesting that this region is not essential for DNA binding or HTH1-HTH2
cooperative interaction. Deletion of a "loop" region between HTH1 and HTH2 was also
performed, and results suggested a role for this region in optimal binding of Rap 1 to tandemly
repeated telomere sequences.
Rapl is a multifunctional protein in S. cerevisiae. It plays a role in chromatin
organization, gene silencing and transcriptional activation. Activation alone takes place using
up to 100 Rapl DNA binding sites on the genome. All of these functions are mediated by Rapl
binding to the DNA duplex, and the Rapl DBD structure must be adaptive to the requirements
of the various cellular processes. This thesis suggests that the HTH1, HTH2, "tail" and "loop"
regions are specifically designed to optimize Rapl function. Cooperative binding to DNA by
HTH1-HTH2 allows a certain degree of degeneracy at high affinity binding sites. "Tail"
interactions, while not essential for DNA binding, maintain binding site specificity at a "core"
ACC sequence. Finally, the "loop" region allows proper alignment of HTH1 and HTH2,
increasing the cooperative association of these two motifs.
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Extent |
13540588 bytes
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Genre | |
Type | |
File Format |
application/pdf
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Language |
eng
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Date Available |
2009-07-23
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Provider |
Vancouver : University of British Columbia Library
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Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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DOI |
10.14288/1.0099529
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URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
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Graduation Date |
2000-11
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Campus | |
Scholarly Level |
Graduate
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Aggregated Source Repository |
DSpace
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Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.