Identification of lysine succinylation as a new post-translational modification.
Identification of lysine succinylation as a new post-translational modification.
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DOI：
10.1038/nchembio.495
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发表时间：
2011-01
影响因子：
14.8
通讯作者：
Zhao, Yingming
中科院分区：
文献类型：
--
作者：
Zhang, Zhihong;Tan, Minjia;Xie, Zhongyu;Dai, Lunzhi;Chen, Yue;Zhao, Yingming
在20个核糖体编码的氨基酸残基中，赖氨酸是最常见的翻译后修饰，具有重要的功能和调控作用。在这里，我们报告鉴定和验证以前未报道的形式的蛋白质翻译后修饰（PTM）：赖氨酸琥珀酰化。通过质谱和蛋白质序列比对初步鉴定了琥珀酰赖氨酸残基。通过western blot分析、琥珀酸同位素在体内标记、MS/MS和HPLC等方法对合成的琥珀酰赖氨酸肽进行了验证。我们进一步表明，赖氨酸琥珀酰化是进化保守的，这种PTM响应不同的生理条件。我们的研究还表明琥珀酰辅酶a可能是赖氨酸琥珀酰化的辅助因子。鉴于赖氨酸琥珀酰化的明显高丰度以及该PTM诱导的显著结构变化，预计赖氨酸琥珀酰化具有重要的细胞功能。
Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially identified by mass spectrometry and protein sequence alignment. The identified succinyllysine peptides derived from in vivo proteins were verified by western blot analysis, in vivo labeling with isotopic succinate, MS/MS and HPLC coelution of their synthetic counterparts. We further show that lysine succinylation is evolutionarily conserved and that this PTM responds to different physiological conditions. Our study also implies that succinyl-CoA might be a cofactor for lysine succinylation. Given the apparent high abundance of lysine succinylation and the significant structural changes induced by this PTM, it is expected that lysine succinylation has important cellular functions.
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影响因子：
7.3
作者：
Norris KL;Lee JY;Yao TP
通讯作者：
Yao TP
影响因子：
4.4
作者：
Zhang K;Chen Y;Zhang Z;Zhao Y
通讯作者：
Zhao Y
影响因子：
7
作者：
Zhang, Junmei;Sprung, Robert;Zhao, Yingming
通讯作者：
Zhao, Yingming
DOI：
10.1073/pnas.82.23.8048
发表时间：
1985-01-01
影响因子：
11.1
作者：
ALLIS, CD;CHICOINE, LG;SCHULMAN, IG
通讯作者：
SCHULMAN, IG
影响因子：
64.5
作者：
Kruse JP;Gu W
通讯作者：
Gu W