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Iron responsive cell surface proteins in Thalassiosira pseudonana as probed by biotinylation and mass spectrometry
Descriptive
TitleInfo
Title
Iron responsive cell surface proteins in Thalassiosira pseudonana as probed by biotinylation and mass spectrometry
Name
(type = personal)
NamePart
(type = family)
New
NamePart
(type = given)
Ashley M.
NamePart
(type = date)
1984-
DisplayForm
Ashley New
Role
RoleTerm
(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Kustka
NamePart
(type = given)
Adam
DisplayForm
Adam Kustka
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
chair
Name
(type = personal)
NamePart
(type = family)
Hansen
NamePart
(type = given)
Darren
DisplayForm
Darren Hansen
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Reinfelder
NamePart
(type = given)
John
DisplayForm
John Reinfelder
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
outside member
Name
(type = corporate)
NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
(type = corporate)
NamePart
Graduate School - Newark
Role
RoleTerm
(authority = RULIB)
school
TypeOfResource
Text
Genre
(authority = marcgt)
theses
OriginInfo
DateCreated
(qualifier = exact)
2013
DateOther
(qualifier = exact);
(type = degree)
2013-05
Place
PlaceTerm
(type = code)
xx
Language
LanguageTerm
(authority = ISO639-2b);
(type = code)
eng
Abstract
(type = abstract)
We investigated the cell-surface enriched proteome of Thalassiosira pseudonana under growth rate limiting (60-70% ยต-max) and replete Fe conditions to better understand transporters that may be involved in Fe uptake. High and low Fe cultures were grown in the presence of 15N-NO3- (>98%) and 14N-NO3- (natural abundance), respectively, enabling relative quantification of proteins. In an effort to identify cell surface proteins, a cell surface labeling and enrichment method was developed and tested. Briefly, cell surface proteins were labeled with a free-amine reactive biotinylation reagent, soluble proteins were removed by membrane lysis and centrifugation, and biotinylated proteins were enriched on a neutravidin resin. Optimal conditions were sought for each of these three processes to increase coverage of cell surface labeled proteins. After elution, extracts were subjected to SDS-PAGE, in-gel tryptic digestion, and separation via liquid chromatography before identification and quantification by tandem mass spectrometry. Identification of cell surface proteins proved problematic due to biotinylation of some intracellular proteins and differential typtic digestion from the presence of the biotin linker arm. We obtained a greater than two-fold increase in abundance of the plasma membrane iron (III) permease (FTR1) under low Fe. A second FTR homolog was identified, indicating the presence of multiple Fe uptake pathways.
Subject
(authority = RUETD)
Topic
Environmental Science
RelatedItem
(type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
(type = RULIB)
ETD
Identifier
ETD_4787
PhysicalDescription
Form
(authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
vi, 79 p. : ill.
Note
(type = degree)
M.S.
Note
(type = bibliography)
Includes bibliographical references
Note
(type = vita)
Includes vita
Note
(type = statement of responsibility)
by Ashley M. New
Subject
(authority = ETD-LCSH)
Topic
Thalassiosira--Research
Subject
(authority = ETD-LCSH)
Topic
Thalassiosira--Effect of iron on
Subject
(authority = ETD-LCSH)
Topic
Mass spectrometry
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10002600001.ETD.000068739
RelatedItem
(type = host)
TitleInfo
Title
Graduate School - Newark Electronic Theses and Dissertations
Identifier
(type = local)
rucore10002600001
Location
PhysicalLocation
(authority = marcorg);
(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T3HQ3XH1
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
RightsDeclaration
(ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder
(type = personal)
Name
FamilyName
New
GivenName
Ashley
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
(encoding = w3cdtf);
(qualifier = exact);
(point = start)
2013-05-01 10:23:57
AssociatedEntity
Name
Ashley New
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - Newark
AssociatedObject
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.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
RULTechMD
(ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem
(VERSION = 5.1)
windows xp
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