메뉴 건너뛰기




Volumn 80, Issue , 2013, Pages 43-54

MS3 fragmentation patterns of monomethylarginine species and the quantification of all methylarginine species in yeast using MRM3

Author keywords

Arginine methyltransferase; Delta monomethyarginine; Epigenetics; MRM cubed; MS cubed; Saccharomyces cerevisiae

Indexed keywords

6 N,N' DIMETHYLARGININE; DEUTERIUM; FUNGAL PROTEIN; ION; METHYL GROUP; N(G) METHYLARGININE; N(G),N(G) DIMETHYLARGININE; ARGININE; DIMETHYLARGININE; N,N-DIMETHYLARGININE;

EID: 84873668916     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.01.003     Document Type: Article
Times cited : (15)

References (35)
  • 3
    • 84868110617 scopus 로고    scopus 로고
    • Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor
    • Neault M., Mallette F.A., Vogel G., Michaud-Levesque J., Richard S. Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor. Nucleic Acids Res 2012, 40:9513-9521.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9513-9521
    • Neault, M.1    Mallette, F.A.2    Vogel, G.3    Michaud-Levesque, J.4    Richard, S.5
  • 4
    • 84868121626 scopus 로고    scopus 로고
    • The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes
    • Stein C., Riedl S., Ruthnick D., Notzold R.R., Bauer U.M. The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes. Nucleic Acids Res 2012, 40:9522-9533.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9522-9533
    • Stein, C.1    Riedl, S.2    Ruthnick, D.3    Notzold, R.R.4    Bauer, U.M.5
  • 5
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acid Res Mol Biol 1998, 61:65-131.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 6
    • 17544376743 scopus 로고    scopus 로고
    • The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae
    • Gary J.D., Lin W.J., Yang M.C., Herschman H.R., Clarke S. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J Biol Chem 1996, 271:12585-12594.
    • (1996) J Biol Chem , vol.271 , pp. 12585-12594
    • Gary, J.D.1    Lin, W.J.2    Yang, M.C.3    Herschman, H.R.4    Clarke, S.5
  • 7
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin W.J., Gary J.D., Yang M.C., Clarke S., Herschman H.R. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem 1996, 271:15034-15044.
    • (1996) J Biol Chem , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 8
    • 33646239364 scopus 로고    scopus 로고
    • Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A
    • Miranda T.B., Sayegh J., Frankel A., Katz J.E., Miranda M., Clarke S. Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A. Biochem J 2006, 395:563-570.
    • (2006) Biochem J , vol.395 , pp. 563-570
    • Miranda, T.B.1    Sayegh, J.2    Frankel, A.3    Katz, J.E.4    Miranda, M.5    Clarke, S.6
  • 9
    • 45449112755 scopus 로고    scopus 로고
    • Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast
    • Sayegh J., Clarke S.G. Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast. Biochem Biophys Res Commun 2008, 372:811-815.
    • (2008) Biochem Biophys Res Commun , vol.372 , pp. 811-815
    • Sayegh, J.1    Clarke, S.G.2
  • 10
    • 0000286998 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids
    • Markley J.L., Bax A., Arata Y., Hilbers C.W., Kaptein R., Sykes B.D., et al. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure Appl Chem 1998, 70:117-142.
    • (1998) Pure Appl Chem , vol.70 , pp. 117-142
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6
  • 11
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase
    • Niewmierzycka A., Clarke S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J Biol Chem 1999, 274:814-824.
    • (1999) J Biol Chem , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 12
    • 0032491583 scopus 로고    scopus 로고
    • Delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins
    • Zobel-Thropp P., Gary J.D., Clarke S. delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins. J Biol Chem 1998, 273:29283-29286.
    • (1998) J Biol Chem , vol.273 , pp. 29283-29286
    • Zobel-Thropp, P.1    Gary, J.D.2    Clarke, S.3
  • 13
    • 0037013283 scopus 로고    scopus 로고
    • Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2
    • Chern M.K., Chang K.N., Liu L.F., Tam T.C., Liu Y.C., Liang Y.L., et al. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J Biol Chem 2002, 277:15345-15353.
    • (2002) J Biol Chem , vol.277 , pp. 15345-15353
    • Chern, M.K.1    Chang, K.N.2    Liu, L.F.3    Tam, T.C.4    Liu, Y.C.5    Liang, Y.L.6
  • 14
    • 84862834055 scopus 로고    scopus 로고
    • Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation
    • Young B.D., Weiss D.I., Zurita-Lopez C.I., Webb K.J., Clarke S.G., McBride A.E. Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation. Biochemistry 2012, 51:5091-5104.
    • (2012) Biochemistry , vol.51 , pp. 5091-5104
    • Young, B.D.1    Weiss, D.I.2    Zurita-Lopez, C.I.3    Webb, K.J.4    Clarke, S.G.5    McBride, A.E.6
  • 15
    • 79953296231 scopus 로고    scopus 로고
    • The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis
    • Leiper J., Nandi M. The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis. Nat Rev Drug Discov 2011, 10:277-291.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 277-291
    • Leiper, J.1    Nandi, M.2
  • 16
    • 40749091589 scopus 로고    scopus 로고
    • N(delta)-Methylated l-arginine derivatives and their effects on the nitric oxide generating system
    • Kotthaus J., Schade D., Topker-Lehmann K., Beitz E., Clement B. N(delta)-Methylated l-arginine derivatives and their effects on the nitric oxide generating system. Bioorg Med Chem 2008, 16:2305-2312.
    • (2008) Bioorg Med Chem , vol.16 , pp. 2305-2312
    • Kotthaus, J.1    Schade, D.2    Topker-Lehmann, K.3    Beitz, E.4    Clement, B.5
  • 17
    • 24344468254 scopus 로고    scopus 로고
    • Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide
    • Pahlich S., Bschir K., Chiavi C., Belyanskaya L., Gehring H. Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. Proteins 2005, 61:164-175.
    • (2005) Proteins , vol.61 , pp. 164-175
    • Pahlich, S.1    Bschir, K.2    Chiavi, C.3    Belyanskaya, L.4    Gehring, H.5
  • 18
    • 67649511917 scopus 로고    scopus 로고
    • Isotope dilution strategies for absolute quantitative proteomics
    • Brun V., Masselon C., Garin J., Dupuis A. Isotope dilution strategies for absolute quantitative proteomics. J Proteomics 2009, 72:740-749.
    • (2009) J Proteomics , vol.72 , pp. 740-749
    • Brun, V.1    Masselon, C.2    Garin, J.3    Dupuis, A.4
  • 19
    • 1942534606 scopus 로고    scopus 로고
    • A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues
    • Brame C.J., Moran M.F., McBroom-Cerajewski L.D. A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues. Rapid Commun Mass Spectrom 2004, 18:877-881.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 877-881
    • Brame, C.J.1    Moran, M.F.2    McBroom-Cerajewski, L.D.3
  • 20
    • 0842310469 scopus 로고    scopus 로고
    • Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS
    • Gehrig P.M., Hunziker P.E., Zahariev S., Pongor S. Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS. J Am Soc Mass Spectrom 2004, 15:142-149.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 142-149
    • Gehrig, P.M.1    Hunziker, P.E.2    Zahariev, S.3    Pongor, S.4
  • 21
    • 60649099160 scopus 로고    scopus 로고
    • Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry
    • Wang H., Straubinger R.M., Aletta J.M., Cao J., Duan X., Yu H., et al. Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry. J Am Soc Mass Spectrom 2009, 20:507-519.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 507-519
    • Wang, H.1    Straubinger, R.M.2    Aletta, J.M.3    Cao, J.4    Duan, X.5    Yu, H.6
  • 22
    • 67650882496 scopus 로고    scopus 로고
    • Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4
    • Lakowski T.M., Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem J 2009, 421:253-261.
    • (2009) Biochem J , vol.421 , pp. 253-261
    • Lakowski, T.M.1    Frankel, A.2
  • 23
    • 78649684721 scopus 로고    scopus 로고
    • Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases
    • Lakowski T.M., t Hart P., Ahern C.A., Martin N.I., Frankel A. Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases. ACS Chem Biol 2010, 5:1053-1063.
    • (2010) ACS Chem Biol , vol.5 , pp. 1053-1063
    • Lakowski, T.M.1    Hart, T.P.2    Ahern, C.A.3    Martin, N.I.4    Frankel, A.5
  • 24
    • 30144443840 scopus 로고    scopus 로고
    • Peptide sequence analysis
    • Medzihradszky K.F. Peptide sequence analysis. Methods Enzymol 2005, 402:209-244.
    • (2005) Methods Enzymol , vol.402 , pp. 209-244
    • Medzihradszky, K.F.1
  • 25
    • 80053009662 scopus 로고    scopus 로고
    • A protein arginine N-methyltransferase 1 (PRMT1) and 2 heteromeric interaction increases PRMT1 enzymatic activity
    • Pak M.L., Lakowski T.M., Thomas D., Vhuiyan M.I., Husecken K., Frankel A. A protein arginine N-methyltransferase 1 (PRMT1) and 2 heteromeric interaction increases PRMT1 enzymatic activity. Biochemistry 2011, 50:8226-8240.
    • (2011) Biochemistry , vol.50 , pp. 8226-8240
    • Pak, M.L.1    Lakowski, T.M.2    Thomas, D.3    Vhuiyan, M.I.4    Husecken, K.5    Frankel, A.6
  • 26
    • 38849108141 scopus 로고    scopus 로고
    • Synthetic approaches to N(delta)-methylated l-arginine, N(omega)-hydroxy-l-arginine, l-citrulline, and N(delta)-cyano-l-ornithine
    • Schade D., Topker-Lehmann K., Kotthaus J., Clement B. Synthetic approaches to N(delta)-methylated l-arginine, N(omega)-hydroxy-l-arginine, l-citrulline, and N(delta)-cyano-l-ornithine. J Org Chem 2008, 73:1025-1030.
    • (2008) J Org Chem , vol.73 , pp. 1025-1030
    • Schade, D.1    Topker-Lehmann, K.2    Kotthaus, J.3    Clement, B.4
  • 28
    • 0037089509 scopus 로고    scopus 로고
    • Determination of arginine, asymmetric dimethylarginine, and symmetric dimethylarginine in human plasma and other biological samples by high-performance liquid chromatography
    • Teerlink T., Nijveldt R.J., de Jong S., van Leeuwen P.A. Determination of arginine, asymmetric dimethylarginine, and symmetric dimethylarginine in human plasma and other biological samples by high-performance liquid chromatography. Anal Biochem 2002, 303:131-137.
    • (2002) Anal Biochem , vol.303 , pp. 131-137
    • Teerlink, T.1    Nijveldt, R.J.2    de Jong, S.3    van Leeuwen, P.A.4
  • 29
    • 71749115867 scopus 로고    scopus 로고
    • Approaches to measuring the activities of protein arginine N-methyltransferases
    • Lakowski T.M., Zurita-Lopez C., Clarke S.G., Frankel A. Approaches to measuring the activities of protein arginine N-methyltransferases. Anal Biochem 2010, 397:1-11.
    • (2010) Anal Biochem , vol.397 , pp. 1-11
    • Lakowski, T.M.1    Zurita-Lopez, C.2    Clarke, S.G.3    Frankel, A.4
  • 30
    • 44349099853 scopus 로고    scopus 로고
    • A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism
    • Lakowski T.M., Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. J Biol Chem 2008, 283:10015-10025.
    • (2008) J Biol Chem , vol.283 , pp. 10015-10025
    • Lakowski, T.M.1    Frankel, A.2
  • 31
    • 78649558287 scopus 로고    scopus 로고
    • Gas-phase structure and fragmentation pathways of singly protonated peptides with N-terminal arginine
    • Bythell B.J., Csonka I.P., Suhai S., Barofsky D.F., Paizs B. Gas-phase structure and fragmentation pathways of singly protonated peptides with N-terminal arginine. J Phys Chem B 2010, 114:15092-15105.
    • (2010) J Phys Chem B , vol.114 , pp. 15092-15105
    • Bythell, B.J.1    Csonka, I.P.2    Suhai, S.3    Barofsky, D.F.4    Paizs, B.5
  • 32
    • 33746335673 scopus 로고    scopus 로고
    • Fragmentations of protonated arginine, lysine and their methylated derivatives: concomitant losses of carbon monoxide or carbon dioxide and an amine
    • Shek P.Y., Zhao J., Ke Y., Siu K.W., Hopkinson A.C. Fragmentations of protonated arginine, lysine and their methylated derivatives: concomitant losses of carbon monoxide or carbon dioxide and an amine. J Phys Chem A 2006, 110:8282-8296.
    • (2006) J Phys Chem A , vol.110 , pp. 8282-8296
    • Shek, P.Y.1    Zhao, J.2    Ke, Y.3    Siu, K.W.4    Hopkinson, A.C.5
  • 33
    • 35448957973 scopus 로고    scopus 로고
    • Fragmentation of protonated dipeptides containing arginine. Effect of activation method
    • Forbes M.W., Jockusch R.A., Young A.B., Harrison A.G. Fragmentation of protonated dipeptides containing arginine. Effect of activation method. J Am Soc Mass Spectrom 2007, 18:1959-1966.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 1959-1966
    • Forbes, M.W.1    Jockusch, R.A.2    Young, A.B.3    Harrison, A.G.4
  • 34
    • 70649087115 scopus 로고    scopus 로고
    • Multiple reaction monitoring cubed for protein quantification at the low nanogram/milliliter level in nondepleted human serum
    • Fortin T., Salvador A., Charrier J.P., Lenz C., Bettsworth F., Lacoux X., et al. Multiple reaction monitoring cubed for protein quantification at the low nanogram/milliliter level in nondepleted human serum. Anal Chem 2009, 81:9343-9352.
    • (2009) Anal Chem , vol.81 , pp. 9343-9352
    • Fortin, T.1    Salvador, A.2    Charrier, J.P.3    Lenz, C.4    Bettsworth, F.5    Lacoux, X.6
  • 35
    • 84861481425 scopus 로고    scopus 로고
    • Rapid, simultaneous and nanomolar determination of pyroglutamic acid and cis-/trans-urocanic acid in human stratum corneum by hydrophilic interaction liquid chromatography (HILIC)-electrospray ionization tandem mass spectrometry
    • Joo K.M., Han J.Y., Son E.D., Nam G.W., Chung H.Y., Jeong H.J. Rapid, simultaneous and nanomolar determination of pyroglutamic acid and cis-/trans-urocanic acid in human stratum corneum by hydrophilic interaction liquid chromatography (HILIC)-electrospray ionization tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 2012, 897:55-63.
    • (2012) J Chromatogr B Analyt Technol Biomed Life Sci , vol.897 , pp. 55-63
    • Joo, K.M.1    Han, J.Y.2    Son, E.D.3    Nam, G.W.4    Chung, H.Y.5    Jeong, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.