Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase

doi:10.3390/ijms22137159

CORC > 深海科学与工程研究所 > 中国科学院深海科学与工程研究所 > 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

	Structure and Function of Piezophilic Hyperthermophilic Pyrococcus yayanosii pApase
	Jin, Zheng 5; Wang, Weiwei 1; Li, Xuegong 6; Zhou, Huan 1; Yi, Gangshun 5; Wang, Qisheng 1; Yu, Feng 1; Xiao, Xiang 2,3,4,5; Liu, Xipeng 4,5
刊名	INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
	2021-07-01
卷号	22 期号:13 页码:17
关键词	Pyrococcus yayanosii pAp pApase DHH phosphoesterase
DOI	10.3390/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.
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关键词	ESCHERICHIA-COLI ; MYCOBACTERIUM-TUBERCULOSIS ; SALT TOLERANCE ; GENE ; SULFOTRANSFERASES ; PHOSPHATASE ; OLIGORIBONUCLEASE ; METABOLISM ; SULFATION ; PATHWAY
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
内容类型	期刊论文
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.Chinese Acad Sci, Shanghai Inst Appl Phys, 239 Zhangheng Rd, Shanghai 201204, Peoples R China 2.Shanghai Jiao Tong Univ, Sch Naval Architecture Ocean & Civil Engn, State Key Lab Ocean Engn, 800 Dong Chuan Rd, Shanghai 200240, Peoples R China 3.Southern Marine Sci & Engn Guangdong Lab Zhuhai, Zhuhai 519080, 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 Life Sci & Biotechnol, State Key Lab Microbial Metab, 800 Dong Chuan Rd, Shanghai 200240, Peoples R China 6.Chinese Acad Sci, Inst Deep Sea Sci & Engn, 28 Luhuitou Rd, Sanya 572000, 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.