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An investigation of cytokinesis in t...
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Epp, J Andrew.
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An investigation of cytokinesis in the yeast Saccharomyces cerevisiae.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
An investigation of cytokinesis in the yeast Saccharomyces cerevisiae./
作者:
Epp, J Andrew.
面頁冊數:
107 p.
附註:
Source: Dissertation Abstracts International, Volume: 60-07, Section: B, page: 3061.
Contained By:
Dissertation Abstracts International60-07B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9935775
ISBN:
0599368969
An investigation of cytokinesis in the yeast Saccharomyces cerevisiae.
Epp, J Andrew.
An investigation of cytokinesis in the yeast Saccharomyces cerevisiae.
- 107 p.
Source: Dissertation Abstracts International, Volume: 60-07, Section: B, page: 3061.
Thesis (Ph.D.)--Harvard University, 1999.
Cytokinesis, occurs by seemingly very different mechanisms among eukaryotes. The identification of increasing numbers of gene families which are involved in cytokinesis has led to the view that in eukaryotes cytokinesis may be fundamentally conserved. It is important to thoroughly characterize the pathways which contribute to cytokinesis, and define the precise roles of the components of those pathways in order to test this premise. This thesis presents evidence of the role of an IQGAP-related protein in cytokinesis in budding yeast. IQG1 is essential for cytokinesis: its deletion results in aberrantly shaped chains of cells which become multinucleate and lyse. Iqg1 co-localizes with, and can induce the assembly of a contractile actomyosin ring which encircles the mother-bud neck. A series of iqg1 deletion constructs was produced, and their effects on viability, cellular morphogenesis, actomyosin ring formation, and Iqg1 localization were examined. A deletion which abolishes Iqg1 and actin assembly into a cytokinetic ring remains partially functional, supporting viability and cytokinesis. Iqg1 localization is also not dependent on the actomyosin ring. These observations in combination with the finding that a deletion of IQG1 is lethal, yet myolDelta strains grow quite well suggests that the actomyosin ring is dispensable for cytokinesis, and that Iqg1 has additional cytokinetic roles. To explore these functions, two multicopy suppressors of an iqg1Delta were isolated---HOF1( CYK2) and CYK3, which likely define cytokinesis pathways independent of the actomyosin ring.
ISBN: 0599368969Subjects--Topical Terms:
1017686
Biology, Cell.
An investigation of cytokinesis in the yeast Saccharomyces cerevisiae.
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Cytokinesis, occurs by seemingly very different mechanisms among eukaryotes. The identification of increasing numbers of gene families which are involved in cytokinesis has led to the view that in eukaryotes cytokinesis may be fundamentally conserved. It is important to thoroughly characterize the pathways which contribute to cytokinesis, and define the precise roles of the components of those pathways in order to test this premise. This thesis presents evidence of the role of an IQGAP-related protein in cytokinesis in budding yeast. IQG1 is essential for cytokinesis: its deletion results in aberrantly shaped chains of cells which become multinucleate and lyse. Iqg1 co-localizes with, and can induce the assembly of a contractile actomyosin ring which encircles the mother-bud neck. A series of iqg1 deletion constructs was produced, and their effects on viability, cellular morphogenesis, actomyosin ring formation, and Iqg1 localization were examined. A deletion which abolishes Iqg1 and actin assembly into a cytokinetic ring remains partially functional, supporting viability and cytokinesis. Iqg1 localization is also not dependent on the actomyosin ring. These observations in combination with the finding that a deletion of IQG1 is lethal, yet myolDelta strains grow quite well suggests that the actomyosin ring is dispensable for cytokinesis, and that Iqg1 has additional cytokinetic roles. To explore these functions, two multicopy suppressors of an iqg1Delta were isolated---HOF1( CYK2) and CYK3, which likely define cytokinesis pathways independent of the actomyosin ring.
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