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dc.contributor.authorWong, Aloysius Tze
dc.contributor.authorGehring, Christoph A
dc.date.accessioned2014-08-27T09:43:04Z
dc.date.available2014-08-27T09:43:04Z
dc.date.issued2013-07-08
dc.identifier.citationWong A, Gehring C (2013) The Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules with functional guanylyl cyclase catalytic centers. Cell Communication and Signaling 11: 48. doi:10.1186/1478-811X-11-48.
dc.identifier.issn1478811X
dc.identifier.pmid23835195
dc.identifier.doi10.1186/1478-811X-11-48
dc.identifier.urihttp://hdl.handle.net/10754/325260
dc.description.abstractBackground: Second messengers link external cues to complex physiological responses. One such messenger, 3',5'-cyclic guanosine monophosphate (cGMP), has been shown to play a key role in many physiological responses in plants. However, in higher plants, guanylyl cyclases (GCs), enzymes that generate cGMP from guanosine-5'-triphosphate (GTP) have remained elusive until recently. GC search motifs constructed from the alignment of known GCs catalytic centers form vertebrates and lower eukaryotes have led to the identification of a number of plant GCs that have been characterized in vitro and in vivo.Presentation of the hypothesis.Recently characterized GCs in Arabidopsis thaliana contributed to the development of search parameters that can identify novel candidate GCs in plants. We hypothesize that there are still a substantial number (> 40) of multi-domain molecules with potentially functional GC catalytic centers in plants that remain to be discovered and characterized. Testing the hypothesis. The hypothesis can be tested, firstly, by computational methods constructing 3D models of selected GC candidates using available crystal structures as templates. Homology modeling must include substrate docking that can provide support for the structural feasibility of the GC catalytic centers in those candidates. Secondly, recombinant peptides containing the GC domain need to be tested in in vitro GC assays such as the enzyme-linked immune-sorbent assay (ELISA) and/or in mass spectrometry based cGMP assays. In addition, quantification of in vivo cGMP transients with fluorescent cGMP-reporter assays in wild-type or selected mutants will help to elucidate the biological role of novel GCs.Implications of the hypothesis.If it turns out that plants do harbor a large number of functional GC domains as part of multi-domain enzymes, then major new insights will be gained into the complex signal transduction pathways that link cGMP to fundamental processes such as ion transport and homeostasis, biotic and abiotic stress responses as well as cGMP-dependent responses to hormones. 2013 Wong and Gehring; licensee BioMed Central Ltd.
dc.language.isoen
dc.publisherSpringer Nature
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights.urihttp://creativecommons.org/licenses/by/2.0
dc.subject3',5'-cyclic guanosine monophosphate (cGMP)
dc.subjectCatalytic center
dc.subjectGC search motif
dc.subjectGuanosine-5'-triphosphate (GTP)
dc.subjectGuanylyl cyclase (GC)
dc.subjectHomology modeling
dc.subjectMolecular docking
dc.subjectguanylate cyclase
dc.subjectproteome
dc.subjectArabidopsis protein
dc.subjectcyclic GMP
dc.subjectguanosine triphosphate
dc.subjectguanylate cyclase
dc.subjectproteome
dc.subjectabiotic stress
dc.subjectArabidopsis thaliana
dc.subjectarticle
dc.subjectbiotic stress
dc.subjectenzyme active site
dc.subjectenzyme activity
dc.subjectenzyme assay
dc.subjectenzyme linked immunosorbent assay
dc.subjectenzyme mechanism
dc.subjectenzyme phosphorylation
dc.subjectenzyme specificity
dc.subjecthydrogen bond
dc.subjectin vitro study
dc.subjectin vivo study
dc.subjection transport
dc.subjectmass spectrometry
dc.subjectmolecular docking
dc.subjectnonhuman
dc.subjectplant response
dc.subjectpriority journal
dc.subjectprotein function
dc.subjectprotein homeostasis
dc.subjectprotein processing
dc.subjectsignal transduction
dc.subjectArabidopsis
dc.subjectchemistry
dc.subjectenzyme active site
dc.subjectenzymology
dc.subjectmetabolism
dc.subjectArabidopsis thaliana
dc.subjectEmbryophyta
dc.subjectEukaryota
dc.subjectVertebrata
dc.subjectArabidopsis
dc.subjectArabidopsis Proteins
dc.subjectCatalytic Domain
dc.subjectCyclic GMP
dc.subjectGuanosine Triphosphate
dc.subjectGuanylate Cyclase
dc.subjectMolecular Docking Simulation
dc.subjectProteome
dc.titleThe Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules with functional guanylyl cyclase catalytic centers
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentMolecular Signalling Group
dc.identifier.journalCell Communication and Signaling
dc.identifier.pmcidPMC3726316
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionUnidad Académica de Sistemas Arrecifales (Puerto Morelos), Instituto de Ciencias Del Mar y Limnología, Universidad Nacional Autõnoma de México, Puerto Morelos, QR 77580, Mexico
dc.contributor.institutionSchool of Natural Sciences, University of California Merced, 5200 North Lake Road, Merced, CA 95343, United States
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personWong, Aloysius Tze
kaust.personGehring, Christoph A.
refterms.dateFOA2018-06-13T14:41:43Z
dc.date.published-online2013-07-08
dc.date.published-print2013


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This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.