Protein l-isoAspartyl Methyltransferase (PIMT) and antioxidants in plants.

4区 医学 Q3 Biochemistry, Genetics and Molecular Biology
Shraboni Ghosh, Manoj Majee
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引用次数: 0

Abstract

All life forms, including plants, accumulate reactive oxygen species (ROS) as a byproduct of metabolism; however, environmental stresses, including abiotic stresses and pathogen attacks, cause enhanced accumulation of ROS in plants. The increased accumulation of ROS often causes oxidative damage to cells. Organisms are able to maintain levels of ROS below permissible limits by several mechanisms, including efficient antioxidant systems. In addition to antioxidant systems, recent studies suggest that protein l-isoaspartyl methyltransferase (PIMT), a highly conserved protein repair enzyme across evolutionary diverse organisms, plays a critical role in maintaining ROS homeostasis by repairing isoaspartyl-mediated damage to antioxidants in plants. Under stress conditions, antioxidant proteins undergo spontaneous isoaspartyl (isoAsp) modification which is often detrimental to protein structure and function. This reduces the catalytic action of antioxidants and disturbs the ROS homeostasis of cells. This chapter focuses on PIMT and its interaction with antioxidants in plants, where PIMT constitutes a secondary level of protection by shielding a primary level of antioxidants from dysfunction and permitting them to guard during unfavorable situations.

蛋白质-异天冬氨酸甲基转移酶(PIMT)与植物抗氧化剂。
所有的生命形式,包括植物,都会积累活性氧(ROS)作为代谢的副产物;然而,环境胁迫,包括非生物胁迫和病原体的攻击,会导致植物体内ROS的积累增加。活性氧积累的增加常常导致细胞氧化损伤。生物体能够通过几种机制,包括有效的抗氧化系统,将活性氧水平维持在允许的限度以下。除了抗氧化系统外,最近的研究表明,蛋白质l-异天冬氨酸甲基转移酶(PIMT)是一种高度保守的蛋白质修复酶,它通过修复异天冬氨酸介导的植物抗氧化剂损伤,在维持ROS稳态中起着关键作用。在应激条件下,抗氧化蛋白发生自发的异天冬氨酸(isoAsp)修饰,这往往对蛋白质的结构和功能有害。这降低了抗氧化剂的催化作用,扰乱了细胞的活性氧稳态。本章重点介绍了植物中PIMT及其与抗氧化剂的相互作用,其中PIMT通过屏蔽初级抗氧化剂免受功能障碍并允许它们在不利情况下进行保护而构成二级保护。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Vitamins and Hormones
Vitamins and Hormones 医学-内分泌学与代谢
CiteScore
3.80
自引率
0.00%
发文量
66
审稿时长
6-12 weeks
期刊介绍: First published in 1943, Vitamins and Hormones is the longest-running serial published by Academic Press. In the early days of the serial, the subjects of vitamins and hormones were quite distinct. The Editorial Board now reflects expertise in the field of hormone action, vitamin action, X-ray crystal structure, physiology, and enzyme mechanisms. Vitamins and Hormones continues to publish cutting-edge reviews of interest to endocrinologists, biochemists, nutritionists, pharmacologists, cell biologists, and molecular biologists. Others interested in the structure and function of biologically active molecules like hormones and vitamins will, as always, turn to this series for comprehensive reviews by leading contributors to this and related disciplines.
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