Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro
Type
ArticleAuthors
Mulaudzi, TakalaniLudidi, Ndiko N.
Ruzvidzo, Oziniel
Morse, Monique V.
Hendricks, Nicolette R.
Iwuoha, Emmanuel Iheanyichukwu
Gehring, Christoph A

KAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Molecular Signalling Group
Date
2011-07-31Online Publication Date
2011-07-31Print Publication Date
2011-09-02Permanent link to this record
http://hdl.handle.net/10754/561865
Metadata
Show full item recordAbstract
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.2011.07.023Sponsors
This work was supported by the South African National Research Foundation.Publisher
WileyJournal
FEBS LettersPubMed ID
21820435ae974a485f413a2113503eed53cd6c53
10.1016/j.febslet.2011.07.023
Scopus Count
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