Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice
Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice
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DOI：
10.1074/jbc.m609778200
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发表时间：
2007-06-08
影响因子：
4.8
通讯作者：
Bedford, Mark T.
中科院分区：
文献类型：
--
作者：
Swiercz, Rafal;Cheng, Donghang;Bedford, Mark T.
PRMT3是存在于细胞质中的I型精氨酸甲基转移酶。发现这种胞质PRMT3的大部分与核糖体相关。它通过与rpS2（也是其底物）的相互作用与核糖体相连。在这里，我们发现PRMT3靶向破坏的小鼠胚胎尺寸很小，但在出生后存活，并在成年后达到正常尺寸，从而显示出分钟样特征。核糖体蛋白rpS2在不存在PRMT3的情况下是低甲基化的，这表明它是真正的体内PRMT3底物，不能被其他PRMT修饰。最后，40 S、60 S和80 S单体和多聚核糖体的水平不受PRMT3损失的影响，但存在另外的尚未鉴定的蛋白质，其与也是专用PRMT3底物的核糖体共断裂。
PRMT3 is a type I arginine methyltransferase that resides in the cytoplasm. A large proportion of this cystosolic PRMT3 is found associated with ribosomes. It is tethered to the ribosomes through its interaction with rpS2, which is also its substrate. Here we show that mouse embryos with a targeted disruption of PRMT3 are small in size but survive after birth and attain a normal size in adulthood, thus displaying Minute-like characteristics. The ribosome protein rpS2 is hypomethylated in the absence of PRMT3, demonstrating that it is a bona fide, in vivo PRMT3 substrate that cannot be modified by other PRMTs. Finally, the levels 40 S, 60 S, and 80 S monosomes and polyribosomes are unaffected by the loss of PRMT3, but there are additional as yet unidentified proteins that co-fractionate with ribosomes that are also dedicated PRMT3 substrates.