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Structural basis of interaction between flagellar type iii atpase FliI and flagellar export chaperone FliT

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Title
Structural basis of interaction between flagellar type iii atpase FliI and flagellar export chaperone FliT
Name (type = personal)
NamePart (type = family)
Khanra
NamePart (type = given)
Nandish Kumar
NamePart (type = date)
1984-
DisplayForm
Nandish Kumar Khanra
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Kalodimos
NamePart (type = given)
Dr. Charalampos
DisplayForm
Dr. Charalampos Kalodimos
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Baum
NamePart (type = given)
Dr. Jean
DisplayForm
Dr. Jean Baum
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Case
NamePart (type = given)
Dr. David
DisplayForm
Dr. David Case
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Ghose
NamePart (type = given)
Dr. Ranajeet
DisplayForm
Dr. Ranajeet Ghose
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 - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (encoding = w3cdtf); (qualifier = exact)
2015
DateOther (qualifier = exact); (type = degree)
2015-01
CopyrightDate (encoding = w3cdtf); (qualifier = exact)
2015
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
Bacterial flagella are complex macro-molecular machines consisting of more than thirty different proteins. The bulk of the flagellum functions in the cell exterior. Therefore, the flagellar component proteins have to be exported during its biosynthesis. Bacteria develop flagella specific type III export pathways for the delivery of flagellar proteins outside the cytoplasm. The flagellar proteins are synthesized in the cytosol and are translocated through the central flagellar channel via a dedicated export apparatus to the distal growing end for the construction of the flagellum. The inner-membrane associated ATPase of flagellar export apparatus, FliI, is considered to be one of the central components in the export process. FliI is a Walker-type ATPase and functions as a hexamer. FliT is the flagellar export chaperone for the flagellar cap-forming protein FliD. It prevents premature aggregation of FliD in the cytosol and facilitates the export of FliD through the export channel. The interaction between FliT and FliI is crucial for the transport of FliD. We have studied the interaction between FliI and FliT using solution NMR combined with other biophysical techniques. Our biophysical data show that FliT interacts with the extreme N-terminal residues of FliI. FliT inhibits the enzymatic activity of FliI by disrupting FliI dimer. FliT is the only flagellar export chaperone known to inhibit the ATPase activity of FliI. We have determined the solution structure of FliI-FliT complex that provides the first high-resolution structure of any chaperone-ATPase complex of flagellar type III export pathway or type III secretion system in general. We have found that FliI binds to the hydrophobic cleft of FliT and the extreme N-terminal residues of FliI forms a α-helix upon FliT binding. The solution structure of FliI-FliT complex provides structural insight about possible binding interface of FliT with its substrate, FliD. Our NMR data as well as biochemical and bio-informative studies show that FliT might have common binding motif for its cognate substrate, FliD and the ATPase, FliI.
Subject (authority = RUETD)
Topic
Chemistry and Chemical Biology
Subject (authority = ETD-LCSH)
Topic
Flagella (Microbiology)
Subject (authority = ETD-LCSH)
Topic
Adenosine triphosphate
Subject (authority = ETD-LCSH)
Topic
Bacteria
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_6094
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (xxvi, 129 p. : ill.)
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Nandish Kumar Khanra
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3WS8W0W
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Khanra
GivenName
Nandish
MiddleName
Kumar
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-12-21 02:10:26
AssociatedEntity
Name
Nandish Khanra
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
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.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2015-01-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2017-01-30
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 30th, 2017.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
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