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Functional characterization of ADP-r...

Chen, Chih-Ying.

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Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway./
Author:	Chen, Chih-Ying.
Description:	142 p.
Notes:	Source: Dissertation Abstracts International, Volume: 60-06, Section: B, page: 2455.
Contained By:	Dissertation Abstracts International60-06B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9933232
ISBN:	059933942X

Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway.
Chen, Chih-Ying.

Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway. - 142 p.

Source: Dissertation Abstracts International, Volume: 60-06, Section: B, page: 2455.

Thesis (Ph.D.)--Vanderbilt University, 1999.

ADP-ribosylation factor (ARF) is a small GTP-binding protein that is thought to regulate the assembly of coat proteins on transport vesicles. To study the role that ARF plays in the cell, two strategies were exploited in yeast Saccharomyces cerevisiae in this dissertation study. First, the secretory defects exhibited by arf mutants were characterized. We found that arf mutants exhibit 2--5 fold slower transport kinetics for all proteins tested and perturbed Golgi and endosome morphology, suggesting a role for ARF in regulating the function and structure of these organelles. Secondly, we initiated a genetic screen for mutations that exhibit synthetic lethality with an arf1 null allele to identify factors that functionally interact with ARF. Seven genes were defined by complementation tests (SWA1- 7 for synthetically lethal with arf1Delta).

ISBN: 059933942XSubjects--Topical Terms:

1017686
Biology, Cell.

Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway.
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100 1 $a Chen, Chih-Ying. $3 1908491
245 1 0 $a Functional characterization of ADP-ribosylation factor in Saccharomyces cerevisiae: Role for ADP-ribosylation factor in the late secretory pathway.
300 $a 142 p.
500 $a Source: Dissertation Abstracts International, Volume: 60-06, Section: B, page: 2455.
500 $a Director: Todd R. Graham.
502 $a Thesis (Ph.D.)--Vanderbilt University, 1999.
520 $a ADP-ribosylation factor (ARF) is a small GTP-binding protein that is thought to regulate the assembly of coat proteins on transport vesicles. To study the role that ARF plays in the cell, two strategies were exploited in yeast Saccharomyces cerevisiae in this dissertation study. First, the secretory defects exhibited by arf mutants were characterized. We found that arf mutants exhibit 2--5 fold slower transport kinetics for all proteins tested and perturbed Golgi and endosome morphology, suggesting a role for ARF in regulating the function and structure of these organelles. Secondly, we initiated a genetic screen for mutations that exhibit synthetic lethality with an arf1 null allele to identify factors that functionally interact with ARF. Seven genes were defined by complementation tests (SWA1- 7 for synthetically lethal with arf1Delta).
520 $a Two SWA genes have been cloned in this study. SWA5 is allelic to the clathrin heavy chain gene (CHC1), which provides in vivo support for a role for ARF in clathrin coat assembly. Mutants carrying this new chc1 allele exhibit a novel protein transport defect that is specific for vacuolar proteins. SWA3/ DRS2 encodes a P-type ATPase and a potential aminophospholipid transporter (or flippase). The drs2 null mutant exhibits several defects that suggest a loss of clathrin function in vivo at the Golgi complex, particularly at nonpermissive temperatures. These results provide the first evidence that an integral membrane protein, possibly also a lipid flippase, is involved in clathrin coated vesicle formation from Golgi membranes.
520 $a The studies of this dissertation provided significant in vivo support for a role for ARF in the late secretory pathway, including recruitment of coat proteins and modulation of phospholipid composition. Furthermore, the identification of a potential membrane modifying enzyme involved in ARF action revealed an exciting novel connection between ARF and membrane structure. membrane structure.
590 $a School code: 0242.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0379
690 $a 0307
690 $a 0369
690 $a 0410
710 2 0 $a Vanderbilt University. $3 1017501
773 0 $t Dissertation Abstracts International $g 60-06B.
790 1 0 $a Graham, Todd R., $e advisor
790 $a 0242
791 $a Ph.D.
792 $a 1999
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9933232