The Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules with functional guanylyl cyclase catalytic centers

Handle URI:
http://hdl.handle.net/10754/325260
Title:
The Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules with functional guanylyl cyclase catalytic centers
Authors:
Wong, Aloysius Tze ( 0000-0002-9105-5845 ) ; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
Background: 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Wong 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.
Publisher:
Springer Nature
Journal:
Cell Communication and Signaling
Issue Date:
8-Jul-2013
DOI:
10.1186/1478-811X-11-48
PubMed ID:
23835195
PubMed Central ID:
PMC3726316
Type:
Article
ISSN:
1478811X
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorWong, Aloysius Tzeen
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2014-08-27T09:43:04Z-
dc.date.available2014-08-27T09:43:04Z-
dc.date.issued2013-07-08en
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.en
dc.identifier.issn1478811Xen
dc.identifier.pmid23835195en
dc.identifier.doi10.1186/1478-811X-11-48en
dc.identifier.urihttp://hdl.handle.net/10754/325260en
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.en
dc.language.isoenen
dc.publisherSpringer Natureen
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.en
dc.rights.urihttp://creativecommons.org/licenses/by/2.0en
dc.subject3',5'-cyclic guanosine monophosphate (cGMP)en
dc.subjectCatalytic centeren
dc.subjectGC search motifen
dc.subjectGuanosine-5'-triphosphate (GTP)en
dc.subjectGuanylyl cyclase (GC)en
dc.subjectHomology modelingen
dc.subjectMolecular dockingen
dc.subjectguanylate cyclaseen
dc.subjectproteomeen
dc.subjectArabidopsis proteinen
dc.subjectcyclic GMPen
dc.subjectguanosine triphosphateen
dc.subjectguanylate cyclaseen
dc.subjectproteomeen
dc.subjectabiotic stressen
dc.subjectArabidopsis thalianaen
dc.subjectarticleen
dc.subjectbiotic stressen
dc.subjectenzyme active siteen
dc.subjectenzyme activityen
dc.subjectenzyme assayen
dc.subjectenzyme linked immunosorbent assayen
dc.subjectenzyme mechanismen
dc.subjectenzyme phosphorylationen
dc.subjectenzyme specificityen
dc.subjecthydrogen bonden
dc.subjectin vitro studyen
dc.subjectin vivo studyen
dc.subjection transporten
dc.subjectmass spectrometryen
dc.subjectmolecular dockingen
dc.subjectnonhumanen
dc.subjectplant responseen
dc.subjectpriority journalen
dc.subjectprotein functionen
dc.subjectprotein homeostasisen
dc.subjectprotein processingen
dc.subjectsignal transductionen
dc.subjectArabidopsisen
dc.subjectchemistryen
dc.subjectenzyme active siteen
dc.subjectenzymologyen
dc.subjectmetabolismen
dc.subjectArabidopsis thalianaen
dc.subjectEmbryophytaen
dc.subjectEukaryotaen
dc.subjectVertebrataen
dc.subjectArabidopsisen
dc.subjectArabidopsis Proteinsen
dc.subjectCatalytic Domainen
dc.subjectCyclic GMPen
dc.subjectGuanosine Triphosphateen
dc.subjectGuanylate Cyclaseen
dc.subjectMolecular Docking Simulationen
dc.subjectProteomeen
dc.titleThe Arabidopsis thaliana proteome harbors undiscovered multi-domain molecules with functional guanylyl cyclase catalytic centersen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalCell Communication and Signalingen
dc.identifier.pmcidPMC3726316en
dc.eprint.versionPublisher's Version/PDFen
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, Mexicoen
dc.contributor.institutionSchool of Natural Sciences, University of California Merced, 5200 North Lake Road, Merced, CA 95343, United Statesen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorWong, Aloysius Tzeen
kaust.authorGehring, Christoph A.en

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