메뉴 건너뛰기




Volumn 323, Issue 2, 2004, Pages 382-387

Spliceosome Sm proteins D1, D3, and B/B′ are asymmetrically dimethylated at arginine residues in the nucleus

Author keywords

Methylation; Methyltransferase; Protein post translational modification; Spliceosome; Splicing

Indexed keywords

AMINO ACID; ARGININE DERIVATIVE; BUFFER; HEMAGGLUTININ; HYDROCHLORIC ACID; ISOPROTEIN; METHIONINE; POLYACRYLAMIDE GEL; SODIUM DIHYDROGEN PHOSPHATE; UREA;

EID: 4544266990     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.107     Document Type: Article
Times cited : (33)

References (27)
  • 1
  • 2
    • 0025173604 scopus 로고
    • Structure of spliceosomal snRNPs and their role in pre-mRNA splicing
    • R. Luhrmann, B. Kastner, and M. Bach Structure of spliceosomal snRNPs and their role in pre-mRNA splicing Biochim. Biophys. Acta 1087 1990 265 292
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 265-292
    • Luhrmann, R.1    Kastner, B.2    Bach, M.3
  • 3
    • 0027651150 scopus 로고
    • Protein composition of mammalian spliceosomal snRNPs
    • C.L. Will, S.E. Behrens, and R. Luhrmann Protein composition of mammalian spliceosomal snRNPs Mol. Biol. Rep. 18 1993 121 126
    • (1993) Mol. Biol. Rep. , vol.18 , pp. 121-126
    • Will, C.L.1    Behrens, S.E.2    Luhrmann, R.3
  • 5
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • C. Kambach, S. Walke, R. Young, J.M. Avis, E. delaFortelle, V.A. Raker, R. Luhrmann, J. Li, and K. Nagai Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs Cell 96 1999 375 387
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    Delafortelle, E.5    Raker, V.A.6    Luhrmann, R.7    Li, J.8    Nagai, K.9
  • 7
    • 0029054377 scopus 로고
    • SnRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm proteinâ€"protein interactions
    • H. Hermann, P. Fabrizio, V.A. Raker, K. Foulaki, H. Hornig, H. Brahms, and R. Luhrmann snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm proteinâ€"protein interactions EMBO J. 9 1995 2076 2088
    • (1995) EMBO J. , vol.9 , pp. 2076-2088
    • Hermann, H.1    Fabrizio, P.2    Raker, V.A.3    Foulaki, K.4    Hornig, H.5    Brahms, H.6    Luhrmann, R.7
  • 8
    • 0027988478 scopus 로고
    • CDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: Evidence for a direct D1-D2 interaction
    • T. Lehmeier, V.A. Raker, H. Hermann, and R. Luhrmann cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction Proc. Natl. Acad. Sci. USA 91 1994 12317 12321
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12317-12321
    • Lehmeier, T.1    Raker, V.A.2    Hermann, H.3    Luhrmann, R.4
  • 9
    • 0030007060 scopus 로고    scopus 로고
    • The snRNP core assembly pathway: Identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro
    • V.A. Raker, G. Plessel, and R. Luhrmann The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro EMBO J. 15 1996 2256 2269
    • (1996) EMBO J. , vol.15 , pp. 2256-2269
    • Raker, V.A.1    Plessel, G.2    Luhrmann, R.3
  • 10
    • 0033104890 scopus 로고    scopus 로고
    • Thirteen anti-Sm monoclonal antibodies immunoprecipitate the three cytoplasmic snRNP core protein precursors in six distinct subsets
    • M. Fury, J. Anderson, P. Ponda, R. Aimes, and G.W. Zieve Thirteen anti-Sm monoclonal antibodies immunoprecipitate the three cytoplasmic snRNP core protein precursors in six distinct subsets J. Autoimmun. 12 1999 91 100
    • (1999) J. Autoimmun. , vol.12 , pp. 91-100
    • Fury, M.1    Anderson, J.2    Ponda, P.3    Aimes, R.4    Zieve, G.W.5
  • 11
    • 0023047717 scopus 로고
    • Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding
    • I. Mattaj Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding Cell 46 1986 905 911
    • (1986) Cell , vol.46 , pp. 905-911
    • Mattaj, I.1
  • 12
    • 0028176685 scopus 로고
    • M3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: Evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain
    • G. Plessel, U. Fischer, and R. Luhrmann m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain Mol. Cell. Biol. 14 1994 4160 4172
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4160-4172
    • Plessel, G.1    Fischer, U.2    Luhrmann, R.3
  • 13
    • 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 protein
    • H. Brahms, L. Meheus, V. De Brabandere, U. Fischer, and R. Luhrmann Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the protein RNA 7 2001 1531 1542
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 14
    • 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
    • H. Brahms, J. Raymackers, A. Union, F. de Keyser, L. Meheus, and R. Luhrmann 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. 275 2000 17122 17129
    • (2000) J. Biol. Chem. , vol.275 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    De Keyser, F.4    Meheus, L.5    Luhrmann, R.6
  • 15
    • 0034602960 scopus 로고    scopus 로고
    • Analysis of the yeast arginine methyltransferase HMT1p/RMT1p and its in vivo function
    • A.E. McBride, V.H. Weiss, H.K. Kim, J.M. Hogle, and P.A. Silver Analysis of the yeast arginine methyltransferase HMT1p/RMT1p and its in vivo function J. Biol. Chem. 275 2000 3128 3136
    • (2000) J. Biol. Chem. , vol.275 , pp. 3128-3136
    • McBride, A.E.1    Weiss, V.H.2    Kim, H.K.3    Hogle, J.M.4    Silver, P.A.5
  • 16
    • 0037244282 scopus 로고    scopus 로고
    • Sam 68 RNA binding protein is an in vivo substrate for protein arginine methyltransferase 1
    • J. Cote, B. Francois-Michel, M.-C. Boulanger, M.T. Bedford, and S. Richard Sam 68 RNA binding protein is an in vivo substrate for protein arginine methyltransferase 1 Mol. Biol. Cell 14 2003 274 287
    • (2003) Mol. Biol. Cell , vol.14 , pp. 274-287
    • Cote, J.1    Francois-Michel, B.2    Boulanger, M.-C.3    Bedford, M.T.4    Richard, S.5
  • 18
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative UsnRNP assembly factor pICln
    • G. Meister, C. Eggert, D. Buhler, H. Brahms, C. Kambach, and U. Fischer Methylation of Sm proteins by a complex containing PRMT5 and the putative UsnRNP assembly factor pICln Curr. Biol. 11 2001 1990 1994
    • (2001) Curr. Biol. , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 19
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • W.J. Friesen, S. Massenet, S. Paushkin, A. Wyce, and G. Dreyfuss SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets Mol. Cell 7 2001 1111 1117
    • (2001) Mol. Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 20
    • 0025159442 scopus 로고
    • Cytoplasmic assembly of snRNP particles from 6S and 20S RNA-free intermediates in L929 mouse fibroblasts
    • R.A. Sauterer, A. Goyal, and G.W. Zieve Cytoplasmic assembly of snRNP particles from 6S and 20S RNA-free intermediates in L929 mouse fibroblasts J. Biol. Chem. 265 1990 1048 1058
    • (1990) J. Biol. Chem. , vol.265 , pp. 1048-1058
    • Sauterer, R.A.1    Goyal, A.2    Zieve, G.W.3
  • 21
    • 0031004560 scopus 로고    scopus 로고
    • Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation
    • S.I. Gunderson, S. Vagner, M. Polycarpou-Schwarz, and I.W. Mattaj Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation Genes Dev. 11 1997 761 773
    • (1997) Genes Dev. , vol.11 , pp. 761-773
    • Gunderson, S.I.1    Vagner, S.2    Polycarpou-Schwarz, M.3    Mattaj, I.W.4
  • 22
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • B.P. Pollack, S.V. Kotenko, W. He, L.S. Izotova, B.L. Barnoski, and S. Pestka The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity J. Biol. Chem. 274 1999 31531 31542
    • (1999) J. Biol. Chem. , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 23
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • T.L. Branscombe, A. Frankel, J.H. Lee, J.R. Cook, Z. Yang, S. Pestka, and S. Clarke PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins J. Biol. Chem. 276 2001 32971 32976
    • (2001) J. Biol. Chem. , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3    Cook, J.R.4    Yang, Z.5    Pestka, S.6    Clarke, S.7
  • 24
    • 0029994329 scopus 로고    scopus 로고
    • A protein that shuttles between the nucleus and cytoplasm is an important mediator of RNA export
    • M.S. Lee, M. Henry, and P.A. Silver A protein that shuttles between the nucleus and cytoplasm is an important mediator of RNA export Genes Dev. 10 1996 1233 1246
    • (1996) Genes Dev. , vol.10 , pp. 1233-1246
    • Lee, M.S.1    Henry, M.2    Silver, P.A.3
  • 26
    • 0037040895 scopus 로고    scopus 로고
    • Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p
    • D.M. Green, K.A. Marfatia, E.B. Crafton, X. Zhang, X. Cheng, and A.H. Corbett Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p J. Biol. Chem. 277 2002 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    Cheng, X.5    Corbett, A.H.6
  • 27
    • 0035106688 scopus 로고    scopus 로고
    • A biochemical function for the Sm complex
    • D. Zhang, N. Abovich, and M. Rosbash A biochemical function for the Sm complex Mol. Cell 7 2001 319 329
    • (2001) Mol. Cell , vol.7 , pp. 319-329
    • Zhang, D.1    Abovich, N.2    Rosbash, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.