Staff View
Gaining insight into the maturation of iron-sulfur (FeS) clusters in staphylococcus aureus by determining the role of DUF59 protein, SufT

Descriptive

TitleInfo
Title
Gaining insight into the maturation of iron-sulfur (FeS) clusters in staphylococcus aureus by determining the role of DUF59 protein, SufT
Name (type = personal)
NamePart (type = family)
Bhatt
NamePart (type = given)
Shiven K.
NamePart (type = date)
1986-
DisplayForm
Shiven K. Bhatt
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Boyd
NamePart (type = given)
Jeffrey M
DisplayForm
Jeffrey M Boyd
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Barkay
NamePart (type = given)
Tamar
DisplayForm
Tamar Barkay
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Zylstra
NamePart (type = given)
Gerben
DisplayForm
Gerben Zylstra
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
School of Graduate Studies
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2018
DateOther (qualifier = exact); (type = degree)
2018-01
CopyrightDate (encoding = w3cdtf); (qualifier = exact)
2018
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
Staphylococcus aureus is a serious mammalian pathogen. For Staphylococcus aureus to successfully inflict pathogenesis upon a host, it is imperative for it to acquire and effectively utilize iron (Fe). Once Fe is internalized, S. aureus utilizes the SUF system to assemble small inorganic cofactors called iron-sulfur (FeS) clusters. FeS clusters have a wide variety of functions in cells, thus, defective FeS cluster assembly results in global metabolic defects. In addition, FeS cluster synthesis and the assembly of FeS proteins is essential in S. aureus and a number of alternate bacterial pathogens suggesting that it is a viable antimicrobial target. Proteins containing DUF59 domains have roles in FeS cluster assembly and are found throughout Eukarya, Bacteria and Archaea. However, the function of DUF59 remains unknown in S. aureus. We have identified the S. aureus SufT, which is composed solely of the DUF59 domain and demonstrated that it has a role in the maturation of iron-sulfur (FeS) proteins.
Subject (authority = RUETD)
Topic
Microbial Biology
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_8669
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (viii, 62 p. : ill.)
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Shiven K. Bhatt
RelatedItem (type = host)
TitleInfo
Title
School of Graduate Studies Electronic Theses and Dissertations
Identifier (type = local)
rucore10001600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3GT5RD3
Genre (authority = ExL-Esploro)
ETD graduate
Back to the top

Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Bhatt
GivenName
Shiven
MiddleName
K.
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2018-01-12 04:36:07
AssociatedEntity
Name
Shiven Bhatt
Role
Copyright holder
Affiliation
Rutgers University. School of Graduate Studies
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
Back to the top

Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
CreatingApplication
Version
1.5
DateCreated (point = end); (encoding = w3cdtf); (qualifier = exact)
2018-01-12T04:20:50
DateCreated (point = end); (encoding = w3cdtf); (qualifier = exact)
2018-01-12T04:20:50
ApplicationName
Microsoft® Word 2010
Back to the top
Version 8.3.13
Rutgers University Libraries - Copyright ©2021