Arginine N-Methyltransferase 1 Is Required for Early Postimplantation Mouse Development, but Cells Deficient in the Enzyme Are Viable

REFERENCES

• Abramovich, C., Yakobson, B., Chebath, J., and Revel, M.. 1997. A protein-ginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. EMBO J. 16:260–266
   PubMed Web of Science ®Google Scholar
• Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J.. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389–3402
   PubMed Web of Science ®Google Scholar
• Byvoet, P., Shepherd, G. R., Hardin, J. M., and Noland, B. J.. 1972. The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells. Arch. Biochem. Biophys. 148:558–567
   PubMed Web of Science ®Google Scholar
• Chen, D., Ma, H., Hong, H., Koh, S. S., Huang, S. M., Schurter, B. T., Aswad, D. W., and Stallcup, M. R.. 1999. Regulation of transcription by a protein methyltransferase. Science 284:2174–2177
   PubMed Web of Science ®Google Scholar
• Chomczynski, P., and Sacchi, N.. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156–159
   PubMed Web of Science ®Google Scholar
• Cimato, T. R., Ettinger, M. J., Zhou, X., and Aletta, J. M.. 1997. Nerve growth factor-specific regulation of protein methylation during neuronal differentiation of PC12 cells. J. Cell Biol. 138:1089–1103
   PubMed Web of Science ®Google Scholar
• Copp, A. J.. 1995. Death before birth: clues from gene knockouts and mutations. Trends Genet. 11:87–93
   PubMed Web of Science ®Google Scholar
• DeGregori, J., Russ, A., von Melchner, H., Rayburn, H., Priyaranjan, P., Jenkins, N. A., Copeland, N. G., and Ruley, H. E.. 1994. A murine homolog of the yeast RNA1 gene is required for postimplantation development. Genes Dev. 8:265–276
   PubMedGoogle Scholar
• Fahrner, K., Hogan, B. L., and Flavell, R. A.. 1987. Transcription of H-2 and Qa genes in embryonic and adult mice. EMBO J. 6:1265–1271
   PubMedGoogle Scholar
• Feinberg, A. P., and Vogelstein, B.. 1984. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137:266–267
   PubMed Web of Science ®Google Scholar
• Gary, J. D., and Clarke, S.. 1998. Protein arginine methyltransferases. Prog. Nucleic Acid Res. 61:65–133
   PubMed Web of Science ®Google Scholar
• Gary, J. D., Lin, W. J., Yang, M. C., Herschman, H. R., and Clarke, S.. 1996. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J. Biol. Chem. 271:12585–12594
   PubMed Web of Science ®Google Scholar
• Henry, M. F., and Silver, P. A.. 1996. A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins. Mol. Cell. Biol. 16:3668–3678
   PubMed Web of Science ®Google Scholar
• Hicks, G. G., Shi, E.-G., Chen, J., Roshon, M., Williamson, D., Scherer, C., and Ruley, H. E.. 1995. Retrovirus gene traps. Methods Enzymol. 254:263–275
   PubMedGoogle Scholar
• Kawasaki, E. S.. 1990. Amplification of RNA PCR protocols: a guide to methods and applications. Innis, M. A., Gelfand, D. H., Sninsky, J. J., and White, T. J. 21–27 Academic Press, San Diego, Calif
   Google Scholar
• Kim, B. R., and Yang, K. H.. 1991. Effects of sinefungin and 5′-deoxy-5′-S-isobutyl-adenosine on lipopolysaccharide-induced proliferation and protein N-methylation of arginyl residues in murine splenic lymphocytes. Toxicol. Lett. 59:109–116
   PubMedGoogle Scholar
• Lin, W. J., Gary, J. D., Yang, M. C., Clarke, S., and Herschman, H. R.. 1996. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 271:15034–15044
   PubMed Web of Science ®Google Scholar
• Lischwe, M. A., Cook, R. G., Ahn, Y. S., Yeoman, L. C., and Busch, H.. 1985. Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23. Biochemistry 24:6025–6028
   PubMedGoogle Scholar
• Lischwe, M. A., Ochs, R. L., Reddy, R., Cook, R. G., Yeoman, L. C., Tan, E. M., Reichlin, M., and Busch, H.. 1985. Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine. J. Biol. Chem. 260:14304–14310
   PubMed Web of Science ®Google Scholar
• Liu, Q., and Dreyfuss, G.. 1995. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 15:2800–2808
   PubMedGoogle Scholar
• Najbauer, J., Johnson, B. A., Young, A. L., and Aswad, D. W.. 1993. Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. J. Biol. Chem. 268:10501–10509
   PubMedGoogle Scholar
• Paik, W. K., Kim, S., and Lee, H. W.. 1972. Protein methylation during the development of rat brain. Biochem. Biophys. Res. Commun. 46:933–941
   PubMedGoogle Scholar
• Pintucci, G., Quarto, N., and Rifkin, D. B.. 1996. Methylation of high molecular weight fibroblast growth factor-2 determines post-translational increases in molecular weight and affects its intracellular distribution. Mol. Biol. Cell 7:1249–1258
   PubMedGoogle Scholar
• Rajpurohit, R., Paik, W. K., and Kim, S.. 1994. Effect of enzymic methylation of heterogeneous ribonucleoprotein particle A1 on its nucleic-acid binding and controlled proteolysis. Biochem. J. 304:903–909
   PubMedGoogle Scholar
• Reddy, S., Rayburn, H., von Melchner, H., and Ruley, H. E.. 1992. Fluorescence-activated sorting of totipotent embryonic stem cells expressing developmentally regulated lacZ fusion genes. Proc. Natl. Acad. Sci. USA 89:6721–6725
   PubMedGoogle Scholar
• Rowe, L. B., Nadeau, J. H., Turner, R., Frankel, W. N., Letts, V. A., Eppig, J. T., Ko, M. S., Thurston, S. J., and Birkenmeier, E. H.. 1994. Maps from two interspecific backcross DNA panels available as a community genetic mapping resource. Mamm. Genome 5:253–274
   PubMed Web of Science ®Google Scholar
• Sambrook, J., Fritsch, E. F., and Maniatis, T.. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Scherer, C. A., Chen, J., Nachabeh, A., Hopkins, N., and Ruley, H. E.. 1989. 1996. Transcriptional specificity of the pluripotent embryonic stem cell. Cell Growth Differ. 7:1393–1401
   Google Scholar
• Scott, H. S., Antonarakis, S. E., Lalioti, M. D., Rossier, C., Silver, P. A., and Henry, M. F.. 1998. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics 48:330–340
   PubMed Web of Science ®Google Scholar
• Shen, E. C., Henry, M. F., Weiss, V. H., Valentini, S. R., Silver, P. A., and Lee, M. S.. 1998. Arginine methylation facilitates the nuclear export of hnRNP proteins. Genes Dev. 12:679–691
   PubMedGoogle Scholar
• Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S., and Herschman, H. R.. 2000. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J. Biol. Chem. 275:7723–7730
   PubMed Web of Science ®Google Scholar
• Tang, J., Gary, J. D., Clarke, S., and Herschman, H. R.. 1998. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273:16935–16945
   PubMed Web of Science ®Google Scholar
• Valentini, S. R., Weiss, V. H., and Silver, P. A.. 1999. Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3′-end formation. RNA 5:272–280
   PubMedGoogle Scholar
• Vanet, A., Plumbridge, J. A., and Alix, J. H.. 1993. Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. J. Bacteriol. 175:7178–7188
   PubMed Web of Science ®Google Scholar
• Williamson, D. J., DeGregori, J., Banik-Maiti, S., and Ruley, H. E.. 2000. hnRNP C is required for postimplantation mouse development but is dispensable for cell viability. Mol. Cell. Biol. 20:4094–4105
   PubMedGoogle Scholar