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

被引：63

作者：

Mulaudzi, Takalani ^{[1
]}

Ludidi, Ndiko ^{[1
]}

Ruzvidzo, Oziniel ^{[2
]}

Morse, Monique ^{[3
]}

Hendricks, Nicolette ^{[4
]}

Iwuoha, Emmanuel ^{[4
]}

Gehring, Chris ^{[1
,5
]}

机构：

[1] Univ Western Cape, Dept Biotechnol, ZA-7535 Bellville, South Africa

[2] North West Univ, Sch Environm & Hlth Sci, ZA-2735 Mmabatho, South Africa

[3] Univ Cape Town, Dept Mol & Cell Biol, ZA-7701 Rondebosch, South Africa

[4] Univ Western Cape, Dept Chem, ZA-7535 Bellville, South Africa

[5] King Abdullah Univ Sci & Technol, Div Chem & Life Sci & Engn, Thuwal 239556900, Saudi Arabia

来源：

FEBS LETTERS | 2011年 / 585卷 / 17期

基金：

新加坡国家研究基金会;

关键词：

Affinity; Cyclic voltammetry; Guanylate cyclase; H-NOX domain; Nitric oxide; Oxygen; Square wave voltammetry; Arabidopsis thaliana; CYCLIC-GMP; CGMP; NO; ACID;

D O I：

10.1016/j.febslet.2011.07.023

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2693 / 2697

页数：5

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