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

doi:10.1016/j.febslet.2011.07.023

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 journal › Article › peer-review

71 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 language	English (US)
Pages (from-to)	2693-2697
Number of pages	5
Journal	FEBS Letters
Volume	585
Issue number	17
DOIs	https://doi.org/10.1016/j.febslet.2011.07.023
State	Published - Jul 31 2011

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This work was supported by the South African National Research Foundation.

ASJC Scopus subject areas

Biochemistry
Structural Biology
Cell Biology
Genetics
Molecular Biology
Biophysics

Access to Document

10.1016/j.febslet.2011.07.023

Cite this

@article{b5f9232134d544bc9d2fc4b312914110,

title = "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. {\textcopyright} 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",

author = "Takalani Mulaudzi and Ludidi, {Ndiko N.} and Oziniel Ruzvidzo and Morse, {Monique V.} and Hendricks, {Nicolette R.} and Iwuoha, {Emmanuel Iheanyichukwu} and Gehring, {Christoph A}",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by the South African National Research Foundation.",

year = "2011",

month = jul,

day = "31",

doi = "10.1016/j.febslet.2011.07.023",

language = "English (US)",

volume = "585",

pages = "2693--2697",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "17",

}

TY - JOUR

T1 - Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro

AU - Mulaudzi, Takalani

AU - Ludidi, Ndiko N.

AU - Ruzvidzo, Oziniel

AU - Morse, Monique V.

AU - Hendricks, Nicolette R.

AU - Iwuoha, Emmanuel Iheanyichukwu

AU - Gehring, Christoph A

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by the South African National Research Foundation.

PY - 2011/7/31

Y1 - 2011/7/31

N2 - 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.

AB - 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.

UR - http://hdl.handle.net/10754/561865

UR - http://doi.wiley.com/10.1016/j.febslet.2011.07.023

UR - http://www.scopus.com/inward/record.url?scp=81155151023&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2011.07.023

DO - 10.1016/j.febslet.2011.07.023

M3 - Article

C2 - 21820435

SN - 0014-5793

VL - 585

SP - 2693

EP - 2697

JO - FEBS Letters

JF - FEBS Letters

IS - 17

ER -

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

Abstract

Bibliographical note

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this