Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase.
Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase.
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嗜压超耐热火球菌 yayanosii pApase 的结构和功能
DOI：
10.3390/ijms22137159
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发表时间：
2021-07-02
影响因子：
5.6
通讯作者：
Liu X
中科院分区：
文献类型：
--
作者：
Jin Z;Wang W;Li X;Zhou H;Yi G;Wang Q;Yu F;Xiao X;Liu X
3 ' -磷酸腺苷5 ' -单磷酸（pAp）是硫酸盐同化和辅酶a代谢的副产物。pAp可通过抑制外核糖核酸酶XRN家族，抑制3′-磷酸腺苷5′-磷酸硫酸酯（PAPS）还原酶和硫代转移酶的活性，调控胁迫条件下基因的表达。在后生动物、植物、酵母和一些细菌中，pAp可通过CysQ转化为5 ' -腺苷单磷酸（AMP）和无机磷酸盐。在一些细菌和古细菌中，来自Asp-His-His （DHH）磷酸酯酶超家族的纳米核糖核酸酶（Nrn）负责回收pAp。此外，氨基水解酶超家族中的组氨酸二醇磷酸酶可以水解pAp。细菌中用于pAp转化的酶及其催化机制已经得到了很好的研究，但这些过程在古细菌中仍不清楚。雅氏焦球菌是一种专性嗜压嗜热古细菌，编码DHH家族的pApase同源物（PyapApase）。生化表征表明，PyapApase能有效地将pAp转化为AMP和磷酸。apo-PyapApase的解析晶体结构与细菌nanoRNaseA （NrnA）相似，但连接DHH和Asp-His-His associated 1 （DHHA1）结构域的α-螺旋连接体略有不同。PyapApase较长的α-螺旋导致DHH和DHHA1结构域之间的底物结合间隙比在细菌NrnA中观察到的更窄。通过对参与配合金属离子与结合底物pAp的保守氨基酸残基的突变分析，证实了PyapApase具有与NrnA相似的离子配位模式，但与底物结合模式略有不同。这些结果为pAp的酶促转换提供了结构和功能上的综合见解，暗示了在超嗜热细胞中硫酸盐同化的潜在功能。
3’-Phosphoadenosine 5’-monophosphate (pAp) is a byproduct of sulfate assimilation and coenzyme A metabolism. pAp can inhibit the activity of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) reductase and sulfotransferase and regulate gene expression under stress conditions by inhibiting XRN family of exoribonucleases. In metazoans, plants, yeast, and some bacteria, pAp can be converted into 5’-adenosine monophosphate (AMP) and inorganic phosphate by CysQ. In some bacteria and archaea, nanoRNases (Nrn) from the Asp-His-His (DHH) phosphoesterase superfamily are responsible for recycling pAp. In addition, histidinol phosphatase from the amidohydrolase superfamily can hydrolyze pAp. The bacterial enzymes for pAp turnover and their catalysis mechanism have been well studied, but these processes remain unclear in archaea. Pyrococcus yayanosii, an obligate piezophilic hyperthermophilic archaea, encodes a DHH family pApase homolog (PyapApase). Biochemical characterization showed that PyapApase can efficiently convert pAp into AMP and phosphate. The resolved crystal structure of apo-PyapApase is similar to that of bacterial nanoRNaseA (NrnA), but they are slightly different in the α-helix linker connecting the DHH and Asp-His-His associated 1 (DHHA1) domains. The longer α-helix of PyapApase leads to a narrower substrate-binding cleft between the DHH and DHHA1 domains than what is observed in bacterial NrnA. Through mutation analysis of conserved amino acid residues involved in coordinating metal ion and binding substrate pAp, it was confirmed that PyapApase has an ion coordination pattern similar to that of NrnA and slightly different substrate binding patterns. The results provide combined structural and functional insight into the enzymatic turnover of pAp, implying the potential function of sulfate assimilation in hyperthermophilic cells.
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影响因子：
4.1
作者：
Linder T
通讯作者：
Linder T
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影响因子：
5.2
作者：
Li Z;Li X;Xiao X;Xu J
通讯作者：
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影响因子：
5.6
作者：
Li Q;Gao Y;Yang A
通讯作者：
Yang A
影响因子：
11.6
作者：
Estavillo, Gonzalo M.;Crisp, Peter A.;Pogson, Barry J.
通讯作者：
Pogson, Barry J.
影响因子：
2.9
作者：
Burkart, MD;Wong, CH
通讯作者：
Wong, CH