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J. Biol. Chem., Vol. 282, Issue 23, 16917-16923, June 8, 2007

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Ribosomal Protein rpS2 Is Hypomethylated in PRMT3-deficient Mice^*

From the University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, Smithville, Texas 78957

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.

Received for publication, October 17, 2006 , and in revised form, April 16, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by the Welch Foundation Grant G-1495. To whom correspondence should be addressed. Tel.: 512-237-9539; 512-237-2475; E-mail: mtbedford{at}mdanderson.org.

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