中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Identification of N-alpha-acetyl-alpha-lysine as a probable thermolyte and its accumulation mechanism in Salinicoccus halodurans H3B36

文献类型:期刊论文

作者Jiang, Kai1,2,3; Xue, Yanfen1,2; Ma, Yanhe1,2
刊名SCIENTIFIC REPORTS
出版日期2015-12-21
卷号5
英文摘要Salinicoccus halodurans H3B36 is a moderate halophile that was isolated from a 3.2-m-deep sediment sample in Qaidam Basin, China. Our results suggest that N-alpha-acetyl-alpha-lysine can accumulate and act as a probable thermolyte in this strain. The accumulation mechanism and biosynthetic pathway for this rare compatible solute were also elucidated. We confirmed that the de novo synthesis pathway of N-alpha-acetyl-alpha-lysine in this strain starts from aspartate and passes through lysine. Through RNA sequencing, we also found an 8-gene cluster (orf_1582-1589) and another gene (orf_2472) that might encode the biosynthesis of N-alpha-acetyl-alpha-lysine in S. halodurans H3B36. Orf_192, orf_193, and orf_1259 might participate in the transportation of precursors for generating N-alpha-acetyl-alpha-lysine under the heat stress. The transcriptome reported here also generated a global view of heat-induced changes and yielded clues for studying the regulation of N-alpha-acetyl-alpha-lysine accumulation. Heat stress triggered a global transcriptional disturbance and generated a series of actions to adapt the strain to heat stress. Furthermore, the transcriptomic results showed that the regulon of RpoN (orf_2534) may be critical to conferring heat stress tolerance and survival to S. halodurans.
WOS标题词Science & Technology
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
关键词[WOS]GENOME-WIDE ANALYSIS ; BETA-LYSINE ; PIPECOLIC ACID ; COMPATIBLE SOLUTES ; ESCHERICHIA-COLI ; BACILLUS-SUBTILIS ; ABC TRANSPORTERS ; GLYCINE BETAINE ; STRESS ; GENE
收录类别SCI
语种英语
WOS记录号WOS:000367070800001
源URL[http://124.16.173.210/handle/834782/1552]  
专题天津工业生物技术研究所_酶工程实验室 马延和 _期刊论文
作者单位1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing, Peoples R China
2.Chinese Acad Sci, Inst Microbiol, Natl Engn Lab Ind Enzymes, Beijing, Peoples R China
3.Univ Chinese Acad Sci, Beijing, Peoples R China
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Jiang, Kai,Xue, Yanfen,Ma, Yanhe. Identification of N-alpha-acetyl-alpha-lysine as a probable thermolyte and its accumulation mechanism in Salinicoccus halodurans H3B36[J]. SCIENTIFIC REPORTS,2015,5.
APA Jiang, Kai,Xue, Yanfen,&Ma, Yanhe.(2015).Identification of N-alpha-acetyl-alpha-lysine as a probable thermolyte and its accumulation mechanism in Salinicoccus halodurans H3B36.SCIENTIFIC REPORTS,5.
MLA Jiang, Kai,et al."Identification of N-alpha-acetyl-alpha-lysine as a probable thermolyte and its accumulation mechanism in Salinicoccus halodurans H3B36".SCIENTIFIC REPORTS 5(2015).

入库方式: OAI收割

来源:天津工业生物技术研究所

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