Dual activities of ACC synthase: Novel clues regarding the molecular evolution of ACS genes.
Dual activities of ACC synthase: Novel clues regarding the molecular evolution of ACS genes.
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ACC 合酶的双重活性：有关 ACS 基因分子进化的新线索
DOI：
10.1126/sciadv.abg8752
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发表时间：
2021-11-12
期刊：
影响因子：
13.6
通讯作者：
Wang NN
中科院分区：
文献类型：
--
作者：
Xu C;Hao B;Sun G;Mei Y;Sun L;Sun Y;Wang Y;Zhang Y;Zhang W;Zhang M;Zhang Y;Wang D;Rao Z;Li X;Shen QJ;Wang NN
种子植物ACC合成酶广泛具有Cβ-S裂解酶活性，提示它们可能是由Cβ-S裂解酶进化而来。乙烯在植物发育中发挥着深远的作用。乙烯生物合成的限速酶是1-氨基环丙烷-1-羧酸(ACC)合成酶，通常认为它是由天冬氨酸氨基转移酶进化而来的单活性酶。在这里，我们证明，除了催化S-腺苷-蛋氨酸转化为乙烯前体Acc外，真正的Acs还广泛地具有C-β-S裂解酶活性。两个N-末端基序，包括一个谷氨酰胺残基，是赋予类ACS蛋白活性所必需的。对不同进化阶段植物中的类ACS蛋白进行的基序和活性分析表明，ACC依赖的途径在种子植物中是独一无二的。根据晶体结构和生化数据，提出了ACSS双重活性的可能催化机理。这些发现不仅扩展了我们目前对ACS功能的理解，而且为ACS基因的进化起源提供了新的见解。
Seed plant ACC synthases widely have Cβ-S lyase activity, suggesting that they may be evolved from Cβ-S lyases. Ethylene plays profound roles in plant development. The rate-limiting enzyme of ethylene biosynthesis is 1-aminocyclopropane-1-carboxylate (ACC) synthase (ACS), which is generally believed to be a single-activity enzyme evolving from aspartate aminotransferases. Here, we demonstrate that, in addition to catalyzing the conversion of S-adenosyl-methionine to the ethylene precursor ACC, genuine ACSs widely have Cβ-S lyase activity. Two N-terminal motifs, including a glutamine residue, are essential for conferring ACS activity to ACS-like proteins. Motif and activity analyses of ACS-like proteins from plants at different evolutionary stages suggest that the ACC-dependent pathway is uniquely developed in seed plants. A putative catalytic mechanism for the dual activities of ACSs is proposed on the basis of the crystal structure and biochemical data. These findings not only expand our current understanding of ACS functions but also provide novel insights into the evolutionary origin of ACS genes.
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