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

Takalani Mulaudzi, Ndiko N. Ludidi, Oziniel Ruzvidzo, Monique V. Morse, Nicolette R. Hendricks, Emmanuel Iheanyichukwu Iwuoha, Christoph A Gehring

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

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.
Original languageEnglish (US)
Pages (from-to)2693-2697
Number of pages5
JournalFEBS Letters
Volume585
Issue number17
DOIs
StatePublished - Jul 31 2011

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Biophysics

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