Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro

Handle URI:
http://hdl.handle.net/10754/561865
Title:
Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro
Authors:
Mulaudzi, Takalani; Ludidi, Ndiko N.; Ruzvidzo, Oziniel; Morse, Monique V.; Hendricks, Nicolette R.; Iwuoha, Emmanuel Iheanyichukwu; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
While there is evidence of nitric oxide (NO)-dependent signalling via the second messenger cyclic guanosine 3′,5′-monophosphate (cGMP) in plants, guanylate cyclases (GCs), enzymes that catalyse the formation of cGMP from guanosine 5′-triphosphate (GTP) have until recently remained elusive and none of the candidates identified to-date are NO-dependent. Using both a GC and heme-binding domain specific (H-NOX) search motif, we have identified an Arabidopsis flavin monooxygenase (At1g62580) and shown electrochemically that it binds NO, has a higher affinity for NO than for O 2 and that this molecule can generate cGMP from GTP in vitro in an NO-dependent manner. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Molecular Signalling Group
Publisher:
Wiley-Blackwell
Journal:
FEBS Letters
Issue Date:
Sep-2011
DOI:
10.1016/j.febslet.2011.07.023
PubMed ID:
21820435
Type:
Article
ISSN:
00145793
Sponsors:
This work was supported by the South African National Research Foundation.
Appears in Collections:
Articles; Bioscience Program; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorMulaudzi, Takalanien
dc.contributor.authorLudidi, Ndiko N.en
dc.contributor.authorRuzvidzo, Ozinielen
dc.contributor.authorMorse, Monique V.en
dc.contributor.authorHendricks, Nicolette R.en
dc.contributor.authorIwuoha, Emmanuel Iheanyichukwuen
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2015-08-03T09:32:49Zen
dc.date.available2015-08-03T09:32:49Zen
dc.date.issued2011-09en
dc.identifier.issn00145793en
dc.identifier.pmid21820435en
dc.identifier.doi10.1016/j.febslet.2011.07.023en
dc.identifier.urihttp://hdl.handle.net/10754/561865en
dc.description.abstractWhile there is evidence of nitric oxide (NO)-dependent signalling via the second messenger cyclic guanosine 3′,5′-monophosphate (cGMP) in plants, guanylate cyclases (GCs), enzymes that catalyse the formation of cGMP from guanosine 5′-triphosphate (GTP) have until recently remained elusive and none of the candidates identified to-date are NO-dependent. Using both a GC and heme-binding domain specific (H-NOX) search motif, we have identified an Arabidopsis flavin monooxygenase (At1g62580) and shown electrochemically that it binds NO, has a higher affinity for NO than for O 2 and that this molecule can generate cGMP from GTP in vitro in an NO-dependent manner. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en
dc.description.sponsorshipThis work was supported by the South African National Research Foundation.en
dc.publisherWiley-Blackwellen
dc.subjectAffinityen
dc.subjectArabidopsis thalianaen
dc.subjectCyclic voltammetryen
dc.subjectGuanylate cyclaseen
dc.subjectH-NOX domainen
dc.subjectNitric oxideen
dc.subjectOxygenen
dc.subjectSquare wave voltammetryen
dc.titleIdentification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitroen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentMolecular Signalling Groupen
dc.identifier.journalFEBS Lettersen
dc.contributor.institutionDepartment of Biotechnology, University of the Western Cape, Private Bag X17, Bellville 7535, South Africaen
dc.contributor.institutionSchool of Environmental and Health Sciences, North-West University, Private Bag X2046, Mmabatho 2735, South Africaen
dc.contributor.institutionDepartment of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch 7701, South Africaen
dc.contributor.institutionDepartment of Chemistry, University of the Western Cape, Private Bag X17, Bellville 7535, South Africaen
kaust.authorGehring, Christoph A.en
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