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

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.

Citation
Mulaudzi, T., Ludidi, N., Ruzvidzo, O., Morse, M., Hendricks, N., Iwuoha, E., & Gehring, C. (2011). Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro. FEBS Letters, 585(17), 2693–2697. doi:10.1016/j.febslet.2011.07.023

Acknowledgements
This work was supported by the South African National Research Foundation.

Publisher
Wiley

Journal
FEBS Letters

DOI
10.1016/j.febslet.2011.07.023

PubMed ID
21820435

Permanent link to this record