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学科主题: 物理化学
题名: Systematic screening of protein modifications in four kinases using affinity enrichment and mass spectrometry analysis with unrestrictive sequence alignment
作者: Zhang, Kai1;  Zhu, Yixin2;  He, Xiwen1;  Zhang, Yukui1, 3
通讯作者: 张凯
关键词: Mass spectrometry ;  Post-translational modifications ;  Phosphorylation ;  Glutathione S-transferase tag ;  Affinity enrichment ;  Kinase
刊名: ANALYTICA CHIMICA ACTA
发表日期: 2011-04-08
DOI: 10.1016/j.aca.2011.02.036
卷: 691, 期:1-2, 页:62-67
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1810
产权排名: 3,4
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Analytical
摘要: Systematic screening of protein modifications in four kinases using affinity enrichment and mass spectrometry analysis with unrestrictive sequence alignment
研究领域[WOS]: Chemistry
英文摘要: Protein kinases transfer phosphate groups from ATP to substrate proteins, they are known to be involved in diverse cellular processes. They are also important therapeutic targets in pharmaceutical design. Previous studies indicated that multiple post-translational modifications (PTMs) exist in kinases in addition to phosphorylation, and these PTMs play an important role in regulating kinases activities. Nevertheless, a comprehensive analysis for PTMs of kinases is insufficient due to technical limitations, which prevent us from better understanding their functional regulation. Here, we have developed a novel strategy that combines glutathione S-transferase tag affinity enrichment with nano-liquid chromatography coupled with tandem mass spectrometry analysis and non-restrictive protein sequence alignment for identification of diverse PTMs in four yeast kinases. The method allows us to enrich and analyze the entire protein isomers and to minimize the loss of all isomers of protein sample during protein purification. In our study, nineteen phosphorylation sites and several other types of FTMs sites were localized in 4 protein kinases. In addition, we found that some interesting mass shifts can not match those of the known FTMs. It suggested the existence of some undescribed PTMs in the proteins. Accordingly, this study showed that the novel strategy holds a great potential for identification of full-spectrum PTMs in proteins. Our data serves as a stepping stone for future functional studies. (C) 2011 Elsevier BM. All rights reserved.
关键词[WOS]: POSTTRANSLATIONAL MODIFICATIONS ;  PHOSPHORYLATION ANALYSIS ;  LYSINE PROPIONYLATION ;  TYROSINE KINASE ;  YEAST ;  IDENTIFICATION ;  CDC15 ;  PHOSPHOPEPTIDES ;  BUTYRYLATION ;  ACETYLATION
语种: 英语
WOS记录号: WOS:000289866100008
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/115326
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Nankai Univ, Dept Chem, Tianjin 300071, Peoples R China
2.Michrom BioResources Inc, Auburn, CA 95603 USA
3.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog Res & Anal Ctr, Dalian 116023, Peoples R China

Recommended Citation:
Zhang, Kai,Zhu, Yixin,He, Xiwen,et al. Systematic screening of protein modifications in four kinases using affinity enrichment and mass spectrometry analysis with unrestrictive sequence alignment[J]. ANALYTICA CHIMICA ACTA,2011,691(1-2):62-67.
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