skip to content
 Mechanisms of plant immune receptor RPM1 and its... Preview this item
ClosePreview this item
Checking...

Mechanisms of plant immune receptor RPM1 and its associated proteins in disease resistance

Author: College of Arts and Sciences, Department of Biology; Dangl, Jeffery L.; Chung, Eui-Hwan
Publisher: University of North Carolina at Chapel Hill University of North Carolina at Chapel Hill 2011-05
Dissertation: Thesis / Dissertation ETD
Edition/Format:   Thesis/dissertation : Thesis/dissertation : eBook : English
Summary:
Plants evolved an immune system to recognize specific pathogens, like animals. Recognition of pathogens in plants results in series of outputs such as generation of reactive oxygen species (ROS), cell wall lignification, and a type of programmed cell death (PCD) called the hypersensitive response (HR). Plant immune receptor proteins, disease resistance (R) proteins, are the necessity for this recognition process.  Read more...
Rating:

(not yet rated) 0 with reviews - Be the first.

Find a copy online

Links to this item

Find a copy in the library

&AllPage.SpinnerRetrieving; Finding libraries that hold this item...

Details

Genre/Form: Dissertation
Material Type: Thesis/dissertation, Internet resource
Document Type: Internet Resource
All Authors / Contributors: College of Arts and Sciences, Department of Biology; Dangl, Jeffery L.; Chung, Eui-Hwan
OCLC Number: 1105759784
Language Note: English

Abstract:

Plants evolved an immune system to recognize specific pathogens, like animals. Recognition of pathogens in plants results in series of outputs such as generation of reactive oxygen species (ROS), cell wall lignification, and a type of programmed cell death (PCD) called the hypersensitive response (HR). Plant immune receptor proteins, disease resistance (R) proteins, are the necessity for this recognition process. The R proteins mediate the plant immune response through direct or indirect recognition of pathogen effector proteins. Our previous works proposed an indirect mode of recognition explaining that R proteins can monitor the host targets (guardees) by guarding them and sense the host targets modification by pathogen effector proteins. Here I present evidence that the Arabidopsis R protein RPM1 and its interacting protein RIN4 form protein complexes in the plant in the presence/absence of bacterial effector proteins implicating that the immune response regulated by R proteins can be controlled via immune complexes. I demonstrate data for RPM1 or RIN4 containing protein complexes by size exclusion chromatography (SEC). I also present data for putative RPM1 interactors by coimmunoprecipitation-coupled liquid chromatography (LC) / mass spectrometry (MS) / MS. With the known RPM1-interacting partner, RIN4, I defined the specific mechanisms of the RPM1-mediated immune response in Arabidopsis through the phosphorylation of the residue threonine 166 in RIN4 triggered by two evolutionarily unrelated bacterial effector proteins, AvrRpm1 and AvrB. Furthermore, I found that an important residue in RIN4, phenylalanine 169, is a key for physical interaction between RPM1 and RIN4 resultant in full accumulation and activation of RPM1 in Arabidopsis.

Reviews

User-contributed reviews
Retrieving GoodReads reviews...
Retrieving DOGObooks reviews...

Tags

Be the first.
Confirm this request

You may have already requested this item. Please select Ok if you would like to proceed with this request anyway.

Linked Data


Primary Entity

<http://www.worldcat.org/oclc/1105759784> # Mechanisms of plant immune receptor RPM1 and its associated proteins in disease resistance
    a schema:CreativeWork, schema:Book, bgn:Thesis ;
    bgn:inSupportOf "Thesis / Dissertation ETD" ;
    library:oclcnum "1105759784" ;
    schema:contributor <http://experiment.worldcat.org/entity/work/data/9356701665#Agent/dangl_jeffery_l> ; # Dangl, Jeffery L.
    schema:contributor <http://experiment.worldcat.org/entity/work/data/9356701665#Agent/college_of_arts_and_sciences_department_of_biology> ; # College of Arts and Sciences, Department of Biology
    schema:creator <http://experiment.worldcat.org/entity/work/data/9356701665#Agent/chung_eui_hwan> ; # Chung, Eui-Hwan
    schema:datePublished "2011" ;
    schema:datePublished "2011/05" ;
    schema:description "Plants evolved an immune system to recognize specific pathogens, like animals. Recognition of pathogens in plants results in series of outputs such as generation of reactive oxygen species (ROS), cell wall lignification, and a type of programmed cell death (PCD) called the hypersensitive response (HR). Plant immune receptor proteins, disease resistance (R) proteins, are the necessity for this recognition process. The R proteins mediate the plant immune response through direct or indirect recognition of pathogen effector proteins. Our previous works proposed an indirect mode of recognition explaining that R proteins can monitor the host targets (guardees) by guarding them and sense the host targets modification by pathogen effector proteins. Here I present evidence that the Arabidopsis R protein RPM1 and its interacting protein RIN4 form protein complexes in the plant in the presence/absence of bacterial effector proteins implicating that the immune response regulated by R proteins can be controlled via immune complexes. I demonstrate data for RPM1 or RIN4 containing protein complexes by size exclusion chromatography (SEC). I also present data for putative RPM1 interactors by coimmunoprecipitation-coupled liquid chromatography (LC) / mass spectrometry (MS) / MS. With the known RPM1-interacting partner, RIN4, I defined the specific mechanisms of the RPM1-mediated immune response in Arabidopsis through the phosphorylation of the residue threonine 166 in RIN4 triggered by two evolutionarily unrelated bacterial effector proteins, AvrRpm1 and AvrB. Furthermore, I found that an important residue in RIN4, phenylalanine 169, is a key for physical interaction between RPM1 and RIN4 resultant in full accumulation and activation of RPM1 in Arabidopsis." ;
    schema:exampleOfWork <http://worldcat.org/entity/work/id/9356701665> ;
    schema:genre "Dissertation" ;
    schema:inLanguage "en" ;
    schema:name "Mechanisms of plant immune receptor RPM1 and its associated proteins in disease resistance" ;
    schema:productID "1105759784" ;
    schema:publication <http://www.worldcat.org/title/-/oclc/1105759784#PublicationEvent/university_of_north_carolina_at_chapel_hilluniversity_of_north_carolina_at_chapel_hill2011_05> ;
    schema:publisher <http://experiment.worldcat.org/entity/work/data/9356701665#Agent/university_of_north_carolina_at_chapel_hill> ; # University of North Carolina at Chapel Hill
    schema:url <https://cdr.lib.unc.edu/concern/dissertations/qn59q410g> ;
    wdrs:describedby <http://www.worldcat.org/title/-/oclc/1105759784> ;
    .


Related Entities

<http://experiment.worldcat.org/entity/work/data/9356701665#Agent/chung_eui_hwan> # Chung, Eui-Hwan
    a bgn:Agent ;
    schema:name "Chung, Eui-Hwan" ;
    .

<http://experiment.worldcat.org/entity/work/data/9356701665#Agent/college_of_arts_and_sciences_department_of_biology> # College of Arts and Sciences, Department of Biology
    a bgn:Agent ;
    schema:name "College of Arts and Sciences, Department of Biology" ;
    .

<http://experiment.worldcat.org/entity/work/data/9356701665#Agent/dangl_jeffery_l> # Dangl, Jeffery L.
    a bgn:Agent ;
    schema:name "Dangl, Jeffery L." ;
    .

<http://experiment.worldcat.org/entity/work/data/9356701665#Agent/university_of_north_carolina_at_chapel_hill> # University of North Carolina at Chapel Hill
    a bgn:Agent ;
    schema:name "University of North Carolina at Chapel Hill" ;
    .


Content-negotiable representations

Close Window

Please sign in to WorldCat 

Don't have an account? You can easily create a free account.