Akmt catalyzes extensive protein lysine methylation in the hyperthermophilic archaeon sulfolobus islandicus but is dispensable for the growth of the organism
文献类型：期刊论文
| 作者 | Chu, Yindi1; Zhu, Yanping2; Chen, Yuling3; Li, Wei4; Zhang, Zhenfeng1; Liu, Di4; Wang, Tongkun1; Ma, Juncai1,4; Deng, Haiteng3; Liu, Zhi-Jie2,5 |
| 刊名 | Molecular & cellular proteomics
 |
| 出版日期 | 2016-09-01 |
| 卷号 | 15期号:9页码:2908-2923 |
| ISSN号 | 1535-9476 |
| DOI | 10.1074/mcp.m115.057778 |
| 通讯作者 | Ouyang, songying(ouyangsy@ibp.ac.cn) ; Huang, li(huangl@sun.im.ac.cn) |
| 英文摘要 | Protein methylation is believed to occur extensively in creanarchaea. recently, akmt, a highly conserved crenarchaeal protein lysine methyltransferase, was identified and shown to exhibit broad substrate specificity in vitro. here, we have constructed an akmt deletion mutant of the hyperthermophilic crenarchaeon sulfolobus islandicus. the mutant was viable but showed a moderately slower growth rate than the parental strain under non-optimal growth conditions. consistent with the moderate effect of the lack of akmt on the growth of the cell, expression of a small number of genes, which encode putative functions in substrate transportation, energy metabolism, transcriptional regulation, stress response proteins, etc, was differentially regulated by more than twofold in the mutant strain, as compared with that in the parental strain. analysis of the methylation of total cellular protein by mass spectrometry revealed that methylated proteins accounted for approximate to 2/3 (1,158/1,751) and approximate to 1/3 (591/1,757) of the identified proteins in the parental and the mutant strains, respectively, indicating that there is extensive protein methylation in s. islandicus and that akmt is a major protein methyltransferase in this organism. no significant sequence preference was detected at the sites of methylation by akmt. methylated lysine residues, when visible in the structure, are all located on the surface of the proteins. the crystal structure of akmt in complex with s-adenosyl-l-methionine (sam) or s-adenosyl homocysteine (sah) reveals that the protein consists of four helices and seven sheets, lacking a substrate recognition domain found in prma, a bacterial homolog of akmt, in agreement with the broad substrate specificity of akmt. our results suggest that akmt may serve a role in maintaining the methylation status of cellular proteins required for the efficient growth of the organism under certain non-optimal conditions. |
| WOS关键词 | THERMOACIDOPHILIC ARCHAEBACTERIUM ; POSTTRANSLATIONAL MODIFICATIONS ; RIBOSOMAL-PROTEINS ; IN-VIVO ; METHYLTRANSFERASE ; SOLFATARICUS ; L11 ; SPECIFICITY ; EXPRESSION ; CHROMATIN |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemical Research Methods |
| 语种 | 英语 |
| WOS记录号 | WOS:000384042300006 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2374206 |
| 专题 | 计算机网络信息中心 |
| 通讯作者 | Ouyang, Songying; Huang, Li |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing, Peoples R China 2.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, 15 Datun Rd, Beijing 100101, Peoples R China 3.Tsinghua Univ, Sch Life Sci, MOE Key Lab Bioinformat, Beijing, Peoples R China 4.Chinese Acad Sci, Inst Microbiol, Network Informat Ctr, Beijing, Peoples R China 5.Shanghai Tech Univ, Human Inst, Shanghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chu, Yindi,Zhu, Yanping,Chen, Yuling,et al. Akmt catalyzes extensive protein lysine methylation in the hyperthermophilic archaeon sulfolobus islandicus but is dispensable for the growth of the organism[J]. Molecular & cellular proteomics,2016,15(9):2908-2923. |
| APA | Chu, Yindi.,Zhu, Yanping.,Chen, Yuling.,Li, Wei.,Zhang, Zhenfeng.,...&Huang, Li.(2016).Akmt catalyzes extensive protein lysine methylation in the hyperthermophilic archaeon sulfolobus islandicus but is dispensable for the growth of the organism.Molecular & cellular proteomics,15(9),2908-2923. |
| MLA | Chu, Yindi,et al."Akmt catalyzes extensive protein lysine methylation in the hyperthermophilic archaeon sulfolobus islandicus but is dispensable for the growth of the organism".Molecular & cellular proteomics 15.9(2016):2908-2923. |
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