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Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice

Rafal Swiercz1, Donghang Cheng, Daehoon Kim

  • 1University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, Smithville, Texas 78957, USA.

The Journal of Biological Chemistry
|April 19, 2007
PubMed

Insights

Protein arginine methyltransferase 3 (PRMT3) disruption in mice causes small size but normal adult growth, revealing its role in ribosome protein methylation. PRMT3 specifically methylates ribosomal protein S2 (rpS2).

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Protein arginine methyltransferase 3 (PRMT3) is a cytoplasmic enzyme.
  • A significant portion of PRMT3 associates with ribosomes, interacting with ribosomal protein S2 (rpS2).
  • rpS2 is a known substrate for PRMT3.

Purpose of the Study:

  • To investigate the in vivo function of PRMT3.
  • To determine the physiological consequences of PRMT3 deficiency.
  • To confirm rpS2 as a direct in vivo substrate of PRMT3.

Main Methods:

  • Generation of PRMT3-deficient mouse embryos.
  • Phenotypic analysis of PRMT3 knockout mice.
  • Analysis of rpS2 methylation status.
  • Ribosome profiling to assess monosome and polysome levels.

Main Results:

  • PRMT3-deficient mouse embryos exhibit a 'Minute-like' phenotype, characterized by small size at birth but normal adult size.
  • Ribosomal protein S2 (rpS2) is hypomethylated in PRMT3-deficient mice, confirming it as a bona fide in vivo substrate.
  • The absence of PRMT3 does not affect the levels of 40S, 60S, and 80S monosomes or polyribosomes.
  • Other unidentified ribosomal proteins are also identified as PRMT3 substrates.

Conclusions:

  • PRMT3 plays a crucial role in the post-translational modification of rpS2.
  • PRMT3 deficiency leads to a specific growth phenotype without disrupting global ribosome biogenesis.
  • Further research is needed to identify additional PRMT3 substrates and their roles in ribosome function.

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