| ZHANG Yalan,CHI Shan,WU Shuangxiu,LIU Cui,YU Jun,WANG Xumin,CHEN Shengping,LIU Tao. 2014. Tryptophan synthase of Phaeophyceae originated from the secondary host nucleus. Acta Oceanologica Sinica, 33(2):63－72 |
| Tryptophan synthase of Phaeophyceae originated from the secondary host nucleus |
| Tryptophan synthase of Phaeophyceae originated from the secondary host nucleus |
| Received:March 27, 2013 Revised:August 05, 2013 |
| DOI：10.1007/s13131-014-0442-5 |
| Key words:tryptophan synthase Rhodophyta Phaeophyceae phylogenetic analysis |
| 中文关键词: tryptophan synthase Rhodophyta Phaeophyceae phylogenetic analysis |
| 基金项目:The National Natural Science Foundation of China under contract Nos 41206116, 31140070 and 31271397; National High Technology Research and Development Program of China under contract No. 2012AA10A406; Technology Project of Ocean and Fisheries of Guangdong Province under contract No. A201201E03; the Fundamental Research Funds for the Central Universities under contract No. 201262003; the algal transcriptome sequencing was supported by 1KP Project (www.onekp.com). |
| Author Name | Affiliation | E-mail | | ZHANG Yalan | College of Marine Life Science, Ocean University of China, Qingdao 266003, China | | | CHI Shan | College of Marine Life Science, Ocean University of China, Qingdao 266003, China | | | WU Shuangxiu | CAS Key Laboratory of Genome Sciences and Information, Beijing Key Laboratory if Genome and precision Medicine Technologies, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China
Beijing Key Laboratory of Functional Genomics for Dao-di Herbs, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China | | | LIU Cui | College of Marine Life Science, Ocean University of China, Qingdao 266003, China | | | YU Jun | CAS Key Laboratory of Genome Sciences and Information, Beijing Key Laboratory if Genome and precision Medicine Technologies, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China
Beijing Key Laboratory of Functional Genomics for Dao-di Herbs, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China | | | WANG Xumin | CAS Key Laboratory of Genome Sciences and Information, Beijing Key Laboratory if Genome and precision Medicine Technologies, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China
Beijing Key Laboratory of Functional Genomics for Dao-di Herbs, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100101, China | wangxm@big.ac.cn | | CHEN Shengping | Guangdong Province Key Laboratory of Functional Molecules in Oceanic Microorganism, Zhong Shan School of Medicine, Sun Yat-Sen University, Guangzhou 510080, China | | | LIU Tao | College of Marine Life Science, Ocean University of China, Qingdao 266003, China | liutao@ouc.edu.cn |
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| Abstract: |
| Tryptophan synthase (TS, EC 4.2.1.20) catalyzes the last two steps of L-tryptophan biosynthesis. In prokaryotes, tryptophan synthase is a multi-enzyme complex, and it consists of α and β subunit which forms an α-ββ-α complex. In fungi and diatoms, TS is a bifunctional enzyme. Because of the limited genomic and transcriptomic data of algae, there are few studies on TS evolution of algae. Here we analyzed the data of the 1000 Plants Project (1KP), and focused on red algae and brown algae. We found out that the TS of Phaeophyceae were fusion genes, which probably originated from the secondary host nucleus, and that the TS of Rhodophyta contained two genes, TSA and TSB, which both display a possible cyanobacterial origin at the time of primary endosymbiosis. In addition, there were two types of TSB genes (TSB1 and TSB2). Through the multiple sequence alignment of TSB proteins, we found several residues conserved in TSB1 but variable in TSB2 which connect with α subunit. The phenomenon may suggest that the TSB2 sequences of Rhodophyta cannot form stable complex with TSA. |
| 中文摘要: |
| Tryptophan synthase (TS, EC 4.2.1.20) catalyzes the last two steps of L-tryptophan biosynthesis. In prokaryotes, tryptophan synthase is a multi-enzyme complex, and it consists of α and β subunit which forms an α-ββ-α complex. In fungi and diatoms, TS is a bifunctional enzyme. Because of the limited genomic and transcriptomic data of algae, there are few studies on TS evolution of algae. Here we analyzed the data of the 1000 Plants Project (1KP), and focused on red algae and brown algae. We found out that the TS of Phaeophyceae were fusion genes, which probably originated from the secondary host nucleus, and that the TS of Rhodophyta contained two genes, TSA and TSB, which both display a possible cyanobacterial origin at the time of primary endosymbiosis. In addition, there were two types of TSB genes (TSB1 and TSB2). Through the multiple sequence alignment of TSB proteins, we found several residues conserved in TSB1 but variable in TSB2 which connect with α subunit. The phenomenon may suggest that the TSB2 sequences of Rhodophyta cannot form stable complex with TSA. |
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