Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo.
Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo.
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DOI：
10.1016/j.chembiol.2011.08.019
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发表时间：
2011-11-23
影响因子：
--
通讯作者：
Kashina A
中科院分区：
文献类型：
--
作者：
Saha S;Wong CC;Xu T;Namgoong S;Zebroski H;Yates JR 3rd;Kashina A
Protein arginylation and arginine methylation are two posttranslational modifications of emerging importance that involve Arg residues and their modifications. To test a hypothesis that posttranslationally added arginines can be methylated, we used high precision mass spectrometry and metabolic labeling to find whether posttranslationally added arginines can serve as methyation sites. We identified a number of proteins in vivo, on which posttranslationally added Arg have undergone mono- and dimethylation. This double modification predominantly affects the chromatin-containing nuclear fraction and likely plays an important regulatory role in chromatin-associated proteins. Moreover, inhibition of arginylation and Arg methylation results in a significant reduction of the nucleus size in cultured cells, suggesting changes in chromatin compaction and nuclear architecture. Our findings suggest a functional link between protein regulation by arginylation and methylation that affects nuclear structure in vivo.
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DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
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通讯作者：
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影响因子：
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作者：
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DOI：
10.1242/dev.022723
发表时间：
2008-12
期刊：
Development (Cambridge, England)
影响因子：
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作者：
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通讯作者：
Kashina A
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影响因子：
14.8
作者：
Xu, Tao;Wong, Catherine C. L.;Kashina, Anna;Yates, John R., III
通讯作者：
Yates, John R., III