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Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase

文献类型：期刊论文

作者Jin, Zheng1; Wang, Weiwei2; Li, Xuegong3; Zhou, Huan2; Yi, Gangshun1; Wang, Qisheng2; Yu, Feng2; Xiao, Xiang1,4,5,6; Liu, Xipeng1,4
刊名INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
出版日期2021-07-01
卷号22期号:13页码:17
关键词Pyrococcus yayanosii pAp pApase DHH phosphoesterase
DOI10.3390/ijms22137159
英文摘要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 alpha-helix linker connecting the DHH and Asp-His-His associated 1 (DHHA1) domains. The longer alpha-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.
WOS关键词ESCHERICHIA-COLI ; MYCOBACTERIUM-TUBERCULOSIS ; SALT TOLERANCE ; GENE ; SULFOTRANSFERASES ; PHOSPHATASE ; OLIGORIBONUCLEASE ; METABOLISM ; SULFATION ; PATHWAY
资助项目National Key R&D Program of China[2018YFC0309806] ; National Key R&D Program of China[2018YFC0310704] ; National Natural Science Foundation of China[U1832161] ; National Natural Science Foundation of China[41921006] ; China Ocean Mineral Resources RD Association[2018YFC0309806] ; China Ocean Mineral Resources RD Association[DY135-B2-12]
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
语种英语
出版者MDPI
WOS记录号WOS:000671211500001
资助机构National Key R&D Program of China ; National Natural Science Foundation of China ; China Ocean Mineral Resources RD Association
源URL[http://ir.idsse.ac.cn/handle/183446/8742]  
专题深海科学研究部_深海生物学研究室_深海微生物细胞生物学研究组
通讯作者Yu, Feng; Xiao, Xiang; Liu, Xipeng
作者单位1.Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, State Key Lab Microbial Metab, 800 Dong Chuan Rd, Shanghai 200240, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Appl Phys, 239 Zhangheng Rd, Shanghai 201204, Peoples R China
3.Chinese Acad Sci, Inst Deep Sea Sci & Engn, 28 Luhuitou Rd, Sanya 572000, Peoples R China
4.Shanghai Jiao Tong Univ, Minist Educ, Joint Int Res Lab Metab & Dev Sci, 800 Dong Chuan Rd, Shanghai 200240, Peoples R China
5.Shanghai Jiao Tong Univ, Sch Naval Architecture Ocean & Civil Engn, State Key Lab Ocean Engn, 800 Dong Chuan Rd, Shanghai 200240, Peoples R China
6.Southern Marine Sci & Engn Guangdong Lab Zhuhai, Zhuhai 519080, Peoples R China
推荐引用方式
GB/T 7714		 Jin, Zheng,Wang, Weiwei,Li, Xuegong,et al. Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase[J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,2021,22(13):17.
APA Jin, Zheng.,Wang, Weiwei.,Li, Xuegong.,Zhou, Huan.,Yi, Gangshun.,...&Liu, Xipeng.(2021).Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase.INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,22(13),17.
MLA Jin, Zheng,et al."Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase".INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 22.13(2021):17.

入库方式： OAI收割

来源：深海科学与工程研究所

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