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The two Tetrahymena thermophila SAS-...
~
Culver, Brady Patrick.
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The two Tetrahymena thermophila SAS-6 homologs perform distinct functions in basal body assembly.
Record Type:
Language materials, printed : Monograph/item
Title/Author:
The two Tetrahymena thermophila SAS-6 homologs perform distinct functions in basal body assembly./
Author:
Culver, Brady Patrick.
Description:
178 p.
Notes:
Source: Dissertation Abstracts International, Volume: 70-04, Section: B, page: 2013.
Contained By:
Dissertation Abstracts International70-04B.
Subject:
Biology, Molecular. -
Online resource:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3354535
ISBN:
9781109115888
The two Tetrahymena thermophila SAS-6 homologs perform distinct functions in basal body assembly.
Culver, Brady Patrick.
The two Tetrahymena thermophila SAS-6 homologs perform distinct functions in basal body assembly.
- 178 p.
Source: Dissertation Abstracts International, Volume: 70-04, Section: B, page: 2013.
Thesis (Ph.D.)--University of Colorado at Boulder, 2009.
Cilia and flagella are structurally and functionally conserved organelles present in basal as well as in all higher eukaryotes. The assembly of cilia requires a microtubule based scaffold called a basal body. The nine-fold symmetry characteristic of basal bodies and the structurally similar centriole is organized around a hub and spoke structure termed the cartwheel. SAS-6 is one of the two clearly conserved components of the cartwheel. In some organisms, overexpression of SAS-6 causes the formation of supernumerary centrioles. In this thesis, I questioned whether the capacity of SAS-6 to initiate centriole assembly is separate from or directly related to its structural role at the cartwheel. To address this question I used Tetrahymena thermophila, which expresses two SAS-6 homologs, TtSAS6a and TtSAS6b.
ISBN: 9781109115888Subjects--Topical Terms:
1017719
Biology, Molecular.
The two Tetrahymena thermophila SAS-6 homologs perform distinct functions in basal body assembly.
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178 p.
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Source: Dissertation Abstracts International, Volume: 70-04, Section: B, page: 2013.
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Adviser: Mark Winey.
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Thesis (Ph.D.)--University of Colorado at Boulder, 2009.
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Cilia and flagella are structurally and functionally conserved organelles present in basal as well as in all higher eukaryotes. The assembly of cilia requires a microtubule based scaffold called a basal body. The nine-fold symmetry characteristic of basal bodies and the structurally similar centriole is organized around a hub and spoke structure termed the cartwheel. SAS-6 is one of the two clearly conserved components of the cartwheel. In some organisms, overexpression of SAS-6 causes the formation of supernumerary centrioles. In this thesis, I questioned whether the capacity of SAS-6 to initiate centriole assembly is separate from or directly related to its structural role at the cartwheel. To address this question I used Tetrahymena thermophila, which expresses two SAS-6 homologs, TtSAS6a and TtSAS6b.
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Cells lacking either TtSAS6a or TtSAS6b are defective in new basal body assembly. TtSas6a localizes to all basal bodies equally, while TtSas6b is enriched at unciliated and assembling basal bodies. Interestingly, overexpression of TtSAS6b but not TtSAS6a, led to the assembly of clusters of new basal bodies in abnormal locations. My data suggest a model where TtSAS6a and TtSAS6b have diverged such that TtSAS6a acts as a structural component of basal bodies, while TtSAS6b influences the location of new basal body assembly.
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The cartwheel is predicted to contain upwards of twenty proteins, however as of February 2009 only five proteins have actually been identified that localize to this structure. I sought to identify other cartwheel proteins through their interaction with Sas6a by immuno-precipitation. Although I did not identify any other basal body proteins with this approach, 3 genes were found to be components of the kinetodesmal fiber. The products of these genes are not immuno-reactive with the Sas6a antibody and may therefore represent bona fide Sas6a containing complexes. In the very least these data suggest that some protein-protein interactions are maintained under the immuno-precipitating conditions.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3354535
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