메뉴 건너뛰기




Volumn 15, Issue 18, 2015, Pages 3232-3243

Expanding the yeast protein arginine methylome

Author keywords

MethylSILAC; Protein arginine methylation; Systems biology; Tandem mass spectrometry; Yeast

Indexed keywords

ARGININE; GLYCINE; PROLINE; RNA BINDING PROTEIN; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84941745554     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500032     Document Type: Article
Times cited : (22)

References (37)
  • 2
    • 0014409081 scopus 로고
    • Protein methylase I. Purification and properties of the enzyme
    • Paik, W. K., Kim, S., Protein methylase I. Purification and properties of the enzyme. J. Biol. Chem. 1968, 243, 2108-2114.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2108-2114
    • Paik, W.K.1    Kim, S.2
  • 3
    • 0034711220 scopus 로고    scopus 로고
    • A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus
    • Zobel-Thropp, P., Yang, M. C., Machado, L., Clarke, S., A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus. J. Biol. Chem. 2000, 275, 37150-37158.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37150-37158
    • Zobel-Thropp, P.1    Yang, M.C.2    Machado, L.3    Clarke, S.4
  • 4
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford, M. T., Clarke, S. G., Protein arginine methylation in mammals: who, what, and why. Mol. Cell 2009, 33, 1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 5
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Côté, J., Richard, S., Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 2005, 280, 28476-28483.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28476-28483
    • Côté, J.1    Richard, S.2
  • 7
    • 84869206964 scopus 로고    scopus 로고
    • A method for large-scale identification of protein arginine methylation
    • Uhlmann, T., Geoghegan, V. L., Thomas, B., Ridlova, G. et al., A method for large-scale identification of protein arginine methylation. Mol. Cell. Proteomics MCP 2012, 11, 1489-1499.
    • (2012) Mol. Cell. Proteomics MCP , vol.11 , pp. 1489-1499
    • Uhlmann, T.1    Geoghegan, V.L.2    Thomas, B.3    Ridlova, G.4
  • 8
    • 84881113123 scopus 로고    scopus 로고
    • Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome
    • Bremang, M., Cuomo, A., Agresta, A. M., Stugiewicz, M. et al., Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome. Mol. Biosyst. 2013, 9, 2231-2247.
    • (2013) Mol. Biosyst. , vol.9 , pp. 2231-2247
    • Bremang, M.1    Cuomo, A.2    Agresta, A.M.3    Stugiewicz, M.4
  • 9
    • 84891801106 scopus 로고    scopus 로고
    • Immunoaffinity enrichment and mass spectrometry analysis of protein methylation
    • Guo, A., Gu, H., Zhou, J., Mulhern, D. et al., Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. Mol. Cell. Proteomics MCP 2014, 13, 372-387.
    • (2014) Mol. Cell. Proteomics MCP , vol.13 , pp. 372-387
    • Guo, A.1    Gu, H.2    Zhou, J.3    Mulhern, D.4
  • 10
    • 84870561934 scopus 로고    scopus 로고
    • Protein arginine methylation in Saccharomyces cerevisiae
    • Low, J. K. K., Wilkins, M. R., Protein arginine methylation in Saccharomyces cerevisiae. FEBS J. 2012, 279, 4423-4443.
    • (2012) FEBS J , vol.279 , pp. 4423-4443
    • Low, J.K.K.1    Wilkins, M.R.2
  • 11
    • 84883805433 scopus 로고    scopus 로고
    • Analysis of the proteome of Saccharomyces cerevisiae for Methylarginine
    • Low, J. K. K., Hart-Smith, G., Erce, M. A., Wilkins, M. R., Analysis of the proteome of Saccharomyces cerevisiae for Methylarginine. J. Proteome Res. 2013, 12, 3884-3899.
    • (2013) J. Proteome Res. , vol.12 , pp. 3884-3899
    • Low, J.K.K.1    Hart-Smith, G.2    Erce, M.A.3    Wilkins, M.R.4
  • 12
  • 13
    • 77649090565 scopus 로고    scopus 로고
    • Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications
    • Pang, C. N. I., Gasteiger, E., Wilkins, M. R., Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications. BMC Genomics 2010, 11, 92.
    • (2010) BMC Genomics , vol.11 , pp. 92
    • Pang, C.N.I.1    Gasteiger, E.2    Wilkins, M.R.3
  • 14
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S.-E., Mittler, G., Mann, M., Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 2004, 1, 119-126.
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.-E.1    Mittler, G.2    Mann, M.3
  • 15
    • 84905281496 scopus 로고    scopus 로고
    • Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest
    • Sylvestersen, K. B., Horn, H., Jungmichel, S., Jensen, L. J., Nielsen, M. L., Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest. Mol. Cell. Proteomics MCP 2014, 13, 2072-2088.
    • (2014) Mol. Cell. Proteomics MCP , vol.13 , pp. 2072-2088
    • Sylvestersen, K.B.1    Horn, H.2    Jungmichel, S.3    Jensen, L.J.4    Nielsen, M.L.5
  • 16
    • 84867345063 scopus 로고    scopus 로고
    • A cross-platform toolkit for mass spectrometry and proteomics
    • Chambers, M. C., Maclean, B., Burke, R., Amodei, D. et al., A cross-platform toolkit for mass spectrometry and proteomics. Nat. Biotechnol. 2012, 30, 918-920.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 918-920
    • Chambers, M.C.1    Maclean, B.2    Burke, R.3    Amodei, D.4
  • 17
    • 84865804286 scopus 로고    scopus 로고
    • Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry
    • Hart-Smith, G., Low, J. K. K., Erce, M. A., Wilkins, M. R., Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry. J. Am. Soc. Mass Spectrom. 2012, 23, 1376-1389.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1376-1389
    • Hart-Smith, G.1    Low, J.K.K.2    Erce, M.A.3    Wilkins, M.R.4
  • 18
    • 0037040895 scopus 로고    scopus 로고
    • Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p
    • Green, D. M., Marfatia, K. A., Crafton, E. B., Zhang, X. et al., Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J. Biol. Chem. 2002, 277, 7752-7760.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7752-7760
    • Green, D.M.1    Marfatia, K.A.2    Crafton, E.B.3    Zhang, X.4
  • 19
    • 34247615911 scopus 로고    scopus 로고
    • Expression of proteins with dimethylarginines in Escherichia coli for protein-protein interaction studies
    • Hsieh, C.-H., Huang, S.-Y., Wu, Y.-C., Liu, L.-F. et al., Expression of proteins with dimethylarginines in Escherichia coli for protein-protein interaction studies. Protein Sci. Publ. Protein Soc. 2007, 16, 919-928.
    • (2007) Protein Sci. Publ. Protein Soc. , vol.16 , pp. 919-928
    • Hsieh, C.-H.1    Huang, S.-Y.2    Wu, Y.-C.3    Liu, L.-F.4
  • 20
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang, D. W., Sherman, B. T., Lempicki, R. A., Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009, 37, 1-13.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 21
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu, Q., Dreyfuss, G., In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 1995, 15, 2800-2808.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 22
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box
    • Kiledjian, M., Dreyfuss, G., Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J. 1992, 11, 2655-2664.
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 23
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G., Dreyfuss, G., Conserved structures and diversity of functions of RNA-binding proteins. Science 1994, 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 24
    • 0033034413 scopus 로고    scopus 로고
    • High affinity interactions of nucleolin with G-G-paired rDNA
    • Hanakahi, L. A., Sun, H., Maizels, N., High affinity interactions of nucleolin with G-G-paired rDNA. J. Biol. Chem. 1999, 274, 15908-15912.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15908-15912
    • Hanakahi, L.A.1    Sun, H.2    Maizels, N.3
  • 25
    • 0029795035 scopus 로고    scopus 로고
    • The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation
    • Mears, W. E., Rice, S. A., The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation. J. Virol. 1996, 70, 7445-7453.
    • (1996) J. Virol. , vol.70 , pp. 7445-7453
    • Mears, W.E.1    Rice, S.A.2
  • 26
    • 0033545875 scopus 로고    scopus 로고
    • Conservation in budding yeast of a kinase specific for SR splicing factors
    • Siebel, C. W., Feng, L., Guthrie, C., Fu, X. D., Conservation in budding yeast of a kinase specific for SR splicing factors. Proc. Natl. Acad. Sci. USA 1999, 96, 5440-5445.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5440-5445
    • Siebel, C.W.1    Feng, L.2    Guthrie, C.3    Fu, X.D.4
  • 27
    • 0035260659 scopus 로고    scopus 로고
    • Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation
    • Gilbert, W., Siebel, C. W., Guthrie, C., Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA 2001, 7, 302-313.
    • (2001) RNA , vol.7 , pp. 302-313
    • Gilbert, W.1    Siebel, C.W.2    Guthrie, C.3
  • 28
    • 33847035256 scopus 로고    scopus 로고
    • The RGG domain of Npl3p recruits Sky1p through docking interactions
    • Lukasiewicz, R., Nolen, B., Adams, J. A., Ghosh, G., The RGG domain of Npl3p recruits Sky1p through docking interactions. J. Mol. Biol. 2007, 367, 249-261.
    • (2007) J. Mol. Biol. , vol.367 , pp. 249-261
    • Lukasiewicz, R.1    Nolen, B.2    Adams, J.A.3    Ghosh, G.4
  • 29
    • 0015296118 scopus 로고
    • The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells
    • Byvoet, P., Shepherd, G. R., Hardin, J. M., Noland, B. J., The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells. Arch. Biochem. Biophys. 1972, 148, 558-567.
    • (1972) Arch. Biochem. Biophys. , vol.148 , pp. 558-567
    • Byvoet, P.1    Shepherd, G.R.2    Hardin, J.M.3    Noland, B.J.4
  • 30
    • 4043129097 scopus 로고    scopus 로고
    • Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors
    • Yu, M. C., Bachand, F., McBride, A. E., Komili, S. et al., Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors. Genes Dev. 2004, 18, 2024-2035.
    • (2004) Genes Dev , vol.18 , pp. 2024-2035
    • Yu, M.C.1    Bachand, F.2    McBride, A.E.3    Komili, S.4
  • 31
    • 0033580840 scopus 로고    scopus 로고
    • Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase
    • Iost, I., Dreyfus, M., Linder, P., Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J. Biol. Chem. 1999, 274, 17677-17683.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 32
    • 74449084888 scopus 로고    scopus 로고
    • Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae
    • Lipson, R. S., Webb, K. J., Clarke, S. G., Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 2010, 391, 1658-1662.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1658-1662
    • Lipson, R.S.1    Webb, K.J.2    Clarke, S.G.3
  • 33
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • Brahms, H., Raymackers, J., Union, A., de Keyser, F. et al., The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 2000, 275, 17122-17129.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    de Keyser, F.4
  • 34
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms, H., Meheus, L., de Brabandere, V., Fischer, U., Lührmann, R., Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA N. Y. N 2001, 7, 1531-1542.
    • (2001) RNA N. Y. N , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    de Brabandere, V.3    Fischer, U.4    Lührmann, R.5
  • 35
    • 13244262884 scopus 로고    scopus 로고
    • Transcriptional regulation by Lge1p requires a function independent of its role in histone H2B ubiquitination
    • Zhang, X., Kolaczkowska, A., Devaux, F., Panwar, S. L. et al., Transcriptional regulation by Lge1p requires a function independent of its role in histone H2B ubiquitination. J. Biol. Chem. 2005, 280, 2759-2770.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2759-2770
    • Zhang, X.1    Kolaczkowska, A.2    Devaux, F.3    Panwar, S.L.4
  • 36
    • 84899627853 scopus 로고    scopus 로고
    • Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding
    • Wei, H.-M., Hu, H.-H., Chang, G.-Y., Lee, Y.-J. et al., Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding. FEBS Lett. 2014, 588, 1542-1548.
    • (2014) FEBS Lett , vol.588 , pp. 1542-1548
    • Wei, H.-M.1    Hu, H.-H.2    Chang, G.-Y.3    Lee, Y.-J.4
  • 37
    • 84881489205 scopus 로고    scopus 로고
    • Global proteomic analysis in trypanosomes reveals unique proteins and conserved cellular processes impacted by arginine methylation
    • Lott, K., Li, J., Fisk, J. C., Wang, H. et al., Global proteomic analysis in trypanosomes reveals unique proteins and conserved cellular processes impacted by arginine methylation. J. Proteomics 2013, 91, 210-225.
    • (2013) J. Proteomics , vol.91 , pp. 210-225
    • Lott, K.1    Li, J.2    Fisk, J.C.3    Wang, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.