详细信息

The cyanobacterial ornithine-ammonia cycle involves an arginine dihydrolase  ( SCI-EXPANDED收录)  

文献类型:期刊文献

英文题名:The cyanobacterial ornithine-ammonia cycle involves an arginine dihydrolase

作者:Zhang, Hao[1,2];Liu, Yujie[1,2];Nie, Xiaoqun[1,2];Liu, Lixia[1];Hua, Qiang[3];Zhao, Guo-Ping[1,4,5,6,7];Yang, Chen[1]

机构:[1]Chinese Acad Sci, Shanghai Inst Plant Physiol & Ecol, CAS Ctr Excellence Mol Plant Sci, CAS Key Lab Synthet Biol, Shanghai, Peoples R China;[2]Univ Chinese Acad Sci, Beijing, Peoples R China;[3]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai, Peoples R China;[4]Fudan Univ, Sch Life Sci, Dept Microbiol & Microbial Engn, State Key Lab Genet Engn, Shanghai, Peoples R China;[5]Fudan Univ, Sch Life Sci, Dept Microbiol & Microbial Engn, Ctr Synthet Biol, Shanghai, Peoples R China;[6]Chinese Univ Hong Kong, Prince Wales Hosp, Dept Microbiol, Shatin, Hong Kong, Peoples R China;[7]Chinese Univ Hong Kong, Prince Wales Hosp, Li Ka Shing Inst Hlth Sci, Shatin, Hong Kong, Peoples R China

年份:2018

卷号:14

期号:6

起止页码:575

外文期刊名:NATURE CHEMICAL BIOLOGY

收录:;WOS:【SCI-EXPANDED(收录号:WOS:000435445100014)】;

基金:The authors thank Y. Shan for technical assistance on hybrid quadrupole-orbitrap MS and J. Zhao for helpful discussions. This work was funded for C.Y. by the National Natural Science Foundation of China (31630003 and 31470168), the National Key R&D Program of China (2016YFC1303303), and the Chinese Academy of Sciences (XDPB0400).

语种:英文

摘要:Living organisms have evolved mechanisms for adjusting their metabolism to adapt to environmental nutrient availability. Terrestrial animals utilize the ornithine-urea cycle to dispose of excess nitrogen derived from dietary protein. Here, we identified an active ornithine-ammonia cycle (OAC) in cyanobacteria through an approach combining dynamic N-15 and C-13 tracers, metabolomics, and mathematical modeling. The pathway starts with carbamoyl phosphate synthesis by the bacterial-and plant-type glutamine-dependent enzyme and ends with conversion of arginine to ornithine and ammonia by a novel arginine dihydrolase. An arginine dihydrolase-deficient mutant showed disruption of OAC and severely impaired cell growth when nitrogen availability oscillated. We demonstrated that the OAC allows for rapid remobilization of nitrogen reserves under starvation and a high rate of nitrogen assimilation and storage after the nutrient becomes available. Thus, the OAC serves as a conduit in the nitrogen storage-and-remobilization machinery in cyanobacteria and enables cellular adaptation to nitrogen fluctuations.

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