Article

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

Department of Biotechnology, University of the Western Cape, Bellville, South Africa.
FEBS letters (impact factor: 3.54). 07/2011; 585(17):2693-7. DOI:10.1016/j.febslet.2011.07.023 pp.2693-7
Source: PubMed

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.

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Keywords

Arabidopsis flavin monooxygenase
 
catalyse
 
elusive
 
GC
 
GCs
 
GTP
 
H-NOX
 
heme-binding domain specific
 
nitric oxide
 
NO-dependent manner
 
plants
 
vitro