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dc.contributor.authorMeier, Stuart
dc.contributor.authorRuzvidzo, Oziniel
dc.contributor.authorMorse, Monique
dc.contributor.authorDonaldson, Lara
dc.contributor.authorKwezi, Lusisizwe
dc.contributor.authorGehring, Christoph A
dc.date.accessioned2014-08-27T09:44:46Z
dc.date.available2014-08-27T09:44:46Z
dc.date.issued2010-01-26
dc.identifier.citationMeier S, Ruzvidzo O, Morse M, Donaldson L, Kwezi L, et al. (2010) The Arabidopsis Wall Associated Kinase-Like 10 Gene Encodes a Functional Guanylyl Cyclase and Is Co-Expressed with Pathogen Defense Related Genes. PLoS ONE 5: e8904. doi:10.1371/journal.pone.0008904.
dc.identifier.issn19326203
dc.identifier.pmid20126659
dc.identifier.doi10.1371/journal.pone.0008904
dc.identifier.urihttp://hdl.handle.net/10754/325282
dc.description.abstractBackground: Second messengers have a key role in linking environmental stimuli to physiological responses. One such messenger, guanosine 3?,5?-cyclic monophosphate (cGMP), has long been known to be an essential signaling molecule in many different physiological processes in higher plants, including biotic stress responses. To date, however, the guanylyl cyclase (GC) enzymes that catalyze the formation of cGMP from GTP have largely remained elusive in higher plants. Principal Findings: We have identified an Arabidopsis receptor type wall associated kinase-like molecule (AtWAKL10) as a candidate GC and provide experimental evidence to show that the intracellular domain of AtWAKL10431-700 can generate cGMP in vitro. Further, we also demonstrate that the molecule has kinase activity indicating that AtWAKL10 is a twin-domain catalytic protein. A co-expression and stimulus-specific expression analysis revealed that AtWAKL10 is consistently coexpressed with well characterized pathogen defense related genes and along with these genes is induced early and sharply in response to a range of pathogens and their elicitors. Conclusions: We demonstrate that AtWAKL10 is a twin-domain, kinase-GC signaling molecule that may function in biotic stress responses that are critically dependent on the second messenger cGMP. © 2010 Meier et al.
dc.language.isoen
dc.publisherPublic Library of Science (PLoS)
dc.rightsMeier et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rightsArchived with thanks to PLoS ONE
dc.subjectcyclic GMP
dc.subjectguanylate cyclase
dc.subjectunclassified drug
dc.subjectvegetable protein
dc.subjectwall associated kinase like 10 protein
dc.subjectArabidopsis protein
dc.subjectguanylate cyclase
dc.subjectprimer DNA
dc.subjectrecombinant protein
dc.subjectArabidopsis
dc.subjectcatalysis
dc.subjectcontrolled study
dc.subjectin vitro study
dc.subjectplant gene
dc.subjectplant stress
dc.subjectprotein domain
dc.subjectprotein expression
dc.subjectamino acid sequence
dc.subjectbiocatalysis
dc.subjectchemistry
dc.subjectelectrospray mass spectrometry
dc.subjectgene expression profiling
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectmicrobiology
dc.subjectmolecular cloning
dc.subjectmolecular genetics
dc.subjectnucleotide sequence
dc.subjectpolymerase chain reaction
dc.subjectArabidopsis
dc.subjectEmbryophyta
dc.subjectAmino Acid Sequence
dc.subjectArabidopsis
dc.subjectArabidopsis Proteins
dc.subjectBase Sequence
dc.subjectBiocatalysis
dc.subjectCloning, Molecular
dc.subjectDNA Primers
dc.subjectGene Expression Profiling
dc.subjectGenes, Plant
dc.subjectGuanylate Cyclase
dc.subjectMolecular Sequence Data
dc.subjectPolymerase Chain Reaction
dc.subjectRecombinant Proteins
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.titleThe arabidopsis wall associated kinase-like 10 gene encodes a functional guanylyl cyclase and is co-expressed with pathogen defense related genes
dc.typeArticle
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.identifier.journalPLoS ONE
dc.identifier.pmcidPMC2811198
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Biotechnology, University of the Western Cape, Bellville, South Africa
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personMeier, Stuart Kurt
kaust.personGehring, Christoph A
refterms.dateFOA2018-06-13T14:47:14Z


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