Protein acetylation: an important mechanism in actinobacteria
文献类型:期刊论文
作者 | Zhang, Huaidong1,2; Xu, Ximing1,3 |
刊名 | Bioscience reports
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出版日期 | 2018-04-27 |
卷号 | 38页码:3 |
ISSN号 | 0144-8463 |
DOI | 10.1042/bsr20170851 |
通讯作者 | Xu, ximing(ximing.xu@univ-paris-diderot.fr) |
英文摘要 | This is a commentary on the research article by lu et al. recently published in bioscience reports. the gcn5-like acetyltransferases with amino acid-binding (act)-gcn5-related n-acetyltransferase (gnat) domain organization have been identified in actinobacteria by lu et al. (2017). the act domain is fused to the gnat domain, conferring amino acid-induced allosteric regulation to these protein acetyltransferases (pat) (amino acid sensing acetyltransferase (aapata)). members of the aapata family share similar secondary structure and are divided into two groups based on the allosteric ligands of the act domain: the asparagine (asn)-activated pata and the cysteine (cys)-activated pata. the former are mainly found in streptomyces; the latter are distributed in other actinobacteria. the authors investigated the effect of asn and cys on the acetylation activity of sven 0867 (svepata, from streptomyces venezuelae dsm 40230) and amir 5672 (amipata, from actinosynnema mirum strain dsm 43827), respectively, as well as the relationship between the structure and function of these enzymes. research history and progress on acetyltransferases and lysine acetylation of proteins were discussed. the activity of pata and acetylation level of proteins may be closely correlated with intracellular concentrations of asn and cys in actinobacteria. |
WOS关键词 | ESCHERICHIA-COLI ; COA SYNTHETASE ; LYSINE ; ACETYLTRANSFERASE ; COBB |
WOS研究方向 | Biochemistry & Molecular Biology ; Cell Biology |
WOS类目 | Biochemistry & Molecular Biology ; Cell Biology |
语种 | 英语 |
WOS记录号 | WOS:000431504200003 |
出版者 | PORTLAND PRESS LTD |
URI标识 | http://www.irgrid.ac.cn/handle/1471x/2373274 |
专题 | 武汉病毒研究所 |
通讯作者 | Xu, Ximing |
作者单位 | 1.Jiangsu Univ Technol, Sch Elect & Informat Engn, Inst Bioinformat & Med Engn, Changzhou 213000, Peoples R China 2.Chinese Acad Sci, Wuhan Inst Virol, Xiao Hong Shan 44, Wuhan 430071, Hubei, Peoples R China 3.Univ Paris Diderot, Sorbonne Paris Cite, CNRS, Unite BFA,UMR 8251, F-75013 Paris, France |
推荐引用方式 GB/T 7714 | Zhang, Huaidong,Xu, Ximing. Protein acetylation: an important mechanism in actinobacteria[J]. Bioscience reports,2018,38:3. |
APA | Zhang, Huaidong,&Xu, Ximing.(2018).Protein acetylation: an important mechanism in actinobacteria.Bioscience reports,38,3. |
MLA | Zhang, Huaidong,et al."Protein acetylation: an important mechanism in actinobacteria".Bioscience reports 38(2018):3. |
入库方式: iSwitch采集
来源:武汉病毒研究所
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