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

FEBS Lett. 2011 Sep 2;585(17):2693-7. doi: 10.1016/j.febslet.2011.07.023. Epub 2011 Jul 31.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / enzymology
  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Electrochemistry
  • Guanylate Cyclase / chemistry
  • Guanylate Cyclase / metabolism*
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Molecular Sequence Data
  • Nitric Oxide / metabolism*
  • Oxygen / metabolism

Substances

  • Arabidopsis Proteins
  • Nitric Oxide
  • Mixed Function Oxygenases
  • NOGC1 protein, Arabidopsis
  • Guanylate Cyclase
  • Oxygen