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Functional characterization of bip2-4, a basl interacting protein, in arabidopsis stomatal development

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TitleInfo
Title
Functional characterization of bip2-4, a basl interacting protein, in arabidopsis stomatal development
Name (type = personal)
NamePart (type = family)
Li
NamePart (type = given)
Dongmeng
NamePart (type = date)
1988-
DisplayForm
Dongmeng Li
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Dong
NamePart (type = given)
Juan
DisplayForm
Juan Dong
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Maliga
NamePart (type = given)
Pal
DisplayForm
Pal Maliga
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Gallavotti
NamePart (type = given)
Andrea
DisplayForm
Andrea Gallavotti
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
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2014
DateOther (qualifier = exact); (type = degree)
2014-10
CopyrightDate (encoding = w3cdtf)
2014
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract
BASL (BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE), a novel intrinsic polarity protein, formulates stomatal stem cell polarization and controls asymmetric cell division (ACD) in Arabidopsis stomatal development. Previous analysis on BASL protein subdomains did not fully elucidate its highly dynamic and dually localized pattern (nucleus and cell peripheral polarity) and its biological function in the stomatal ACD cells. From a genome-wide yeast two-hybrid (Y2H) screening, our lab identified two plant-specific families, BIP1 (BASL Interaction Protein Family 1) and BIP2 (BASL Interaction Protein Family 2), both sharing a common plant-specific BID (BASL Interaction Domain) domain. This work focuses on the BIP2 family, particularly BIP2-4, to investigate where this protein is subcellularly localized and whether this gene family plays a role in stomatal ACD and developmental patterning. The physical interaction between BIP2-4 and BASL was further confirmed with pairwise Y2H tests, Bimolecular Fluorescence Complementation (BiFC) and co-expression assays in tobacco leaves. BiFC assays also demonstrated that in addition to interacting with BASL, BIP2-4 also interacts with the MAPKKK YDA, a recently established polarity protein that interacts with BASL. Intriguingly, the interactions between BASL and BIP2-4 and between YDA and BIP2-4 triggered spontaneous protein co-polarization, suggesting a positive role of BIP2-4 in polarity formation. To genetically investigate the biological functions of the BIP2 family, the new genome editing/mutagenesis technology, CRISPR, was tested and successfully established in the Arabidopsis stomatal system. The employment of this technology provided an efficient solution to overcome genetic redundancy within the BIP2 family for further functional analysis. The BIP2 family has a potential link to the Phosphoinositide (PI) signaling pathway, due to the presence of multiple PI-binding signature domains in their sequences. To connect the possible PI signaling to BIP2, the subcellular localization of BIP2-4 subdomains and three previously established PI biosensors that specifically bind to PI3P, PI4P, or PI(4, 5)P2 were examined and compared in the stomata lineage cells.
Subject (authority = RUETD)
Topic
Plant Biology
Subject (authority = ETD-LCSH)
Topic
Cell division
Subject (authority = ETD-LCSH)
Topic
Arabidopsis
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5994
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (vi, 29 p. : ill.)
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Dongmeng Li
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/T3RV0MCX
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
Li
GivenName
Dongmeng
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-10-01 17:03:34
AssociatedEntity
Name
Dongmeng Li
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)
2014-10-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2016-10-30
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after October 30th, 2016.
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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