Pyruvate-sensitive AOX exists as a non-covalently associated dimer in the homeothermic spadix of the skunk cabbage, Symplocarpus renifolius
Pyruvate-sensitive AOX exists as a non-covalently associated dimer in the homeothermic spadix of the skunk cabbage, Symplocarpus renifolius
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DOI：
10.1016/j.febslet.2007.11.061
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发表时间：
2007-12-22
期刊：
影响因子：
3.5
通讯作者：
Ito, Kikukatsu
中科院分区：
文献类型：
--
作者：
Onda, Yoshihiko;Kato, Yoshiaki;Ito, Kikukatsu
抗氰交替氧化酶（AOX）是一种同源二聚体蛋白，其活性可通过氧化/还原状态和α-酮酸调节。为了进一步阐明AOX在臭甘蓝中的作用，我们对AOX编码基因进行了表达和功能分析。在臭鼬甘蓝的各种组织中，SrAOX转录本被发现在产热肉穗花序中特异性表达。此外，我们的数据表明，SrAOX蛋白存在作为一个非共价相关的二聚体在产热肉穗花序，是丙酮酸比其他羧酸更敏感。我们的研究结果表明，阿托伐他汀介导的modi。SrAOX活性在臭鼬菜的温度调节中起重要作用。(C)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The cyanide-resistant alternative oxidase (AOX) is a homodimeric protein whose activity can be regulated by the oxidation/reduction state and by a-keto acids. To further clarify the role of AOX in the skunk cabbage, Symplocarpus renifolius, we have performed expression and functional analyses of the encoding gene. Among the various tissues in the skunk cabbage, SrAOX transcripts were found to be specifically expressed in the thermogenic spadix. Moreover, our data demonstrate that the SrAOX protein exists as a non-covalently associated dimer in the thermogenic spadix, and is more sensitive to pyruvate than to other carboxylic acids. Our results suggest that the pyruvate-mediated modi. cation of SrAOX activity plays a significant role in thermoregulation in the skunk cabbage. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.