Functional characterization of bip2-4, a basl interacting protein, in arabidopsis stomatal development
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Li, Dongmeng.
Functional characterization of bip2-4, a basl interacting protein, in arabidopsis stomatal development. Retrieved from
https://doi.org/doi:10.7282/T3RV0MCX
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TitleFunctional characterization of bip2-4, a basl interacting protein, in arabidopsis stomatal development
Date Created2014
Other Date2014-10 (degree)
Extent1 online resource (vi, 29 p. : ill.)
DescriptionBASL (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.
NoteM.S.
NoteIncludes bibliographical references
Noteby Dongmeng Li
Genretheses, ETD graduate
Languageeng
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.