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 |
推荐引用方式 GB/T 7714 | 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
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。