Ubiquitin-Like Protein SAMP1 and JAMM/MPN+ Metalloprotease HvJAMM1 Constitute a System for Reversible Regulation of Metabolic Enzyme Activity in Archaea.
Ubiquitin-Like Protein SAMP1 and JAMM/MPN+ Metalloprotease HvJAMM1 Constitute a System for Reversible Regulation of Metabolic Enzyme Activity in Archaea.
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DOI：
10.1371/journal.pone.0128399
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发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Maupin-Furlow JA
中科院分区：
文献类型：
--
作者：
Cao S;Hepowit N;Maupin-Furlow JA
泛素/泛素样蛋白(Ub/Ubl)通过与蛋白质底物的共价键参与多种细胞过程。在这里，我们为调控酶活性的翻译后修饰系统提供了证据，该系统由古生菌Ub1蛋白(SAMP1)和JAMM/MPN+金属蛋白酶(HvJAMM1)组成。研究发现，SAMP1与MPT合成酶大亚基(MoaE)的共价连接抑制了MPT合成酶的活性。HvJAMM1能将共价连接的SAMP1-MoaE裂解到MPT合成酶的SAMP1和MoaE亚基上，提示该金属蛋白酶可使MPT合成酶重新激活。总之，这项研究为Ub/Ubl修饰是一个翻译后过程，可以直接和可逆地调节代谢酶的活性这一广泛的概念提供了新的见解。特别是，我们证明了一种酶(MPT合成酶)活性部位残基上的Ub/Ubl键可以抑制其催化活性，并且该酶可以被JAMM/MPN+金属蛋白酶切割而重新激活。
Ubiquitin/ubiquitin-like (Ub/Ubl) proteins are involved in diverse cellular processes by their covalent linkage to protein substrates. Here, we provide evidence for a post-translational modification system that regulates enzyme activity which is composed of an archaeal Ubl protein (SAMP1) and a JAMM/MPN+ metalloprotease (HvJAMM1). Molybdopterin (MPT) synthase activity was found to be inhibited by covalent linkage of SAMP1 to the large subunit (MoaE) of MPT synthase. HvJAMM1 was shown to cleave the covalently linked inactive form of SAMP1-MoaE to the free functional individual SAMP1 and MoaE subunits of MPT synthase, suggesting reactivation of MPT synthase by this metalloprotease. Overall, this study provides new insight into the broad idea that Ub/Ubl modification is a post-translational process that can directly and reversibly regulate the activity of metabolic enzymes. In particular, we show that Ub/Ubl linkages on the active site residues of an enzyme (MPT synthase) can inhibit its catalytic activity and that the enzyme can be reactivated through cleavage by a JAMM/MPN+ metalloprotease.
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