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Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1
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Descriptive

TitleInfo (displayLabel = Citation Title); (type = uniform)
Title
Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1
Name (ID = NAME001); (type = personal)
NamePart (type = family)
Hashizume
NamePart (type = given)
Kristina Kaori
DisplayForm
Kristina Kaori Hashizume
Role
RoleTerm (authority = RUETD)
author
Name (ID = NAME002); (type = personal)
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Grant
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Barth
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Advisory Committee
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Barth Grant
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chair
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NamePart (type = family)
Kinzy
NamePart (type = given)
Terri
Affiliation
Advisory Committee
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Terri Kinzy
Role
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internal member
Name (ID = NAME004); (type = personal)
NamePart (type = family)
Carr
NamePart (type = given)
Chavela
Affiliation
Advisory Committee
DisplayForm
Chavela Carr
Role
RoleTerm (authority = RULIB)
internal member
Name (ID = NAME005); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (ID = NAME006); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2008
DateOther (qualifier = exact); (type = degree)
2008-05
Language
LanguageTerm
English
PhysicalDescription
Form (authority = marcform)
electronic
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
ix, 68 pages
Abstract
The Sec1/Munc18 (SM) family of proteins is essential for intracellular vesicle trafficking in eukaryotic cells. Sec1, the SM protein at the yeast plasma membrane, is required for membrane fusion leading to secretion and cell growth. Fusion of exocytic vesicles targeted to the plasma membrane occurs in two stages. The vesicle is first tethered to the membrane by a protein complex called the exocyst. Essential membrane-associated proteins known as the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) located on both the plasma membrane and the vesicle assemble together to form a stable four-helix bundle called the SNARE complex. In the second step, Sec1 binds to the assembled SNARE complex and there is fusion of the two membranes.
Sec1 has been shown to bind the SNARE complex, but the exact role and mechanism of Sec1 function remains unknown. In this study, site-directed mutagenesis was used to investigate the significance of highly conserved salt bridges in SM proteins and define the SNARE complex binding surface on Sec1 with data from random mutants studied by Yi-Shan Cheng and Jenna Hutton. In addition, Sec1 mutants with a novel phenotype were generated that may support a role for Sec1 in vesicle tethering.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references (p. 64-68).
Subject (ID = SUBJ1); (authority = RUETD)
Topic
Microbiology and Molecular Genetics
Subject (ID = SUBJ2); (authority = ETD-LCSH)
Topic
Membrane proteins
Subject (ID = SUBJ3); (authority = ETD-LCSH)
Topic
Mutagenesis
Subject (ID = SUBJ4); (authority = ETD-LCSH)
Topic
Yeast fungi
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17323
Identifier
ETD_838
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3WD40XX
Genre (authority = ExL-Esploro)
ETD graduate
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Rights

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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
Kristina Hashizume
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
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Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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Technical

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application/x-tar
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6106624
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windows xp
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application/x-tar
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