메뉴 건너뛰기




Volumn 342, Issue 2, 2006, Pages 472-481

FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

Author keywords

propeller; F box; FBXO11; FLJ12673; Immunolocalization; Methylation; PRMT; Protein arginine methyltransferase; Structure modeling; Symmetric dimethylarginine; Type II; Zinc finger

Indexed keywords

DIMETHYLARGININASE; FBX011 PROTEIN; N(G),N(G) DIMETHYLARGININE; PRMT9 PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 33344475410     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.01.167     Document Type: Article
Times cited : (123)

References (39)
  • 1
    • 0034733748 scopus 로고    scopus 로고
    • Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3
    • J. Tang, P.N. Kao, and H.R. Herschman Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3 J. Biol. Chem. 275 2000 19866 19876
    • (2000) J. Biol. Chem. , vol.275 , pp. 19866-19876
    • Tang, J.1    Kao, P.N.2    Herschman, H.R.3
  • 2
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
    • M.R. Pawlak, C.A. Scherer, J. Chen, M.J. Roshon, and H.E. Ruley Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable Mol. Cell Biol. 20 2000 4859 4869
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, H.E.5
  • 3
    • 0027156138 scopus 로고
    • 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. Najbauer, B.A. Johnson, A.L. Young, and D.W. Aswad 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 1993 10501 10509
    • (1993) J. Biol. Chem. , vol.268 , pp. 10501-10509
    • Najbauer, J.1    Johnson, B.A.2    Young, A.L.3    Aswad, D.W.4
  • 4
    • 0033049526 scopus 로고    scopus 로고
    • Involvement of receptor-bound protein methyltransferase PRMT1 in antiviral and antiproliferative effects of type I interferons
    • L. Altschuler, J.O. Wook, D. Gurari, J. Chebath, and M. Revel Involvement of receptor-bound protein methyltransferase PRMT1 in antiviral and antiproliferative effects of type I interferons J. Interferon Cytokine Res. 19 1999 189 195
    • (1999) J. Interferon Cytokine Res. , vol.19 , pp. 189-195
    • Altschuler, L.1    Wook, J.O.2    Gurari, D.3    Chebath, J.4    Revel, M.5
  • 5
    • 0032521176 scopus 로고    scopus 로고
    • Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)
    • H.S. Scott, S.E. Antonarakis, M.D. Lalioti, C. Rossier, P.A. Silver, and M.F. Henry Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2) Genomics 48 1998 330 340
    • (1998) Genomics , vol.48 , pp. 330-340
    • Scott, H.S.1    Antonarakis, S.E.2    Lalioti, M.D.3    Rossier, C.4    Silver, P.A.5    Henry, M.F.6
  • 6
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α
    • C. Qi, J. Chang, Y. Zhu, A.V. Yeldandi, S.M. Rao, and Y.J. Zhu Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α J. Biol. Chem. 277 2002 28624 28630
    • (2002) J. Biol. Chem. , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 7
    • 0032479171 scopus 로고    scopus 로고
    • PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
    • J. Tang, J.D. Gary, S. Clarke, and H.R. Herschman 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 1998 16935 16945
    • (1998) J. Biol. Chem. , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 8
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • X. Zhang, L. Zhou, and X. Cheng Crystal structure of the conserved core of protein arginine methyltransferase PRMT3 EMBO J. 19 2000 3509 3519
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 9
    • 0034731452 scopus 로고    scopus 로고
    • Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
    • D. Chen, S.M. Huang, and M.R. Stallcup Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300 J. Biol. Chem. 275 2000 40810 40816
    • (2000) J. Biol. Chem. , vol.275 , pp. 40810-40816
    • Chen, D.1    Huang, S.M.2    Stallcup, M.R.3
  • 10
    • 0037195877 scopus 로고    scopus 로고
    • Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function
    • C. Teyssier, D. Chen, and M.R. Stallcup Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function J. Biol. Chem. 277 2002 46066 46072
    • (2002) J. Biol. Chem. , vol.277 , pp. 46066-46072
    • Teyssier, C.1    Chen, D.2    Stallcup, M.R.3
  • 11
    • 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
  • 14
    • 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
  • 16
    • 0032080214 scopus 로고    scopus 로고
    • PICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology
    • G. Krapivinsky, W. Pu, K. Wickman, L. Krapivinsky, and D.E. Clapham pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology J. Biol. Chem. 273 1998 10811 10814
    • (1998) J. Biol. Chem. , vol.273 , pp. 10811-10814
    • Krapivinsky, G.1    Pu, W.2    Wickman, K.3    Krapivinsky, L.4    Clapham, D.E.5
  • 17
    • 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
    • H. Brahms, L. Meheus, B. de, V.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 SMN protein RNA 7 2001 1531 1542
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De, B.3    Fischer, V.U.4    Luhrmann, R.5
  • 18
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP 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 U snRNP 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
    • 0034864677 scopus 로고    scopus 로고
    • The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1
    • J. Rho, S. Choi, Y.R. Seong, J. Choi, and D.S. Im The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1 J. Virol. 75 2001 8031 8044
    • (2001) J. Virol. , vol.75 , pp. 8031-8044
    • Rho, J.1    Choi, S.2    Seong, Y.R.3    Choi, J.4    Im, D.S.5
  • 22
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Y.T. Kwak, J. Guo, S. Prajapati, K.J. Park, R.M. Surabhi, B. Miller, P. Gehrig, and R.B. Gaynor Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties Mol. Cell 11 2003 1055 1066
    • (2003) Mol. Cell , vol.11 , pp. 1055-1066
    • Kwak, Y.T.1    Guo, J.2    Prajapati, S.3    Park, K.J.4    Surabhi, R.M.5    Miller, B.6    Gehrig, P.7    Gaynor, R.B.8
  • 23
    • 0142123234 scopus 로고    scopus 로고
    • MSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad
    • S. Pal, R. Yun, A. Datta, L. Lacomis, H. Erdjument-Bromage, J. Kumar, P. Tempst, and S. Sif mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad Mol. Cell Biol. 23 2003 7475 7487
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7475-7487
    • Pal, S.1    Yun, R.2    Datta, A.3    Lacomis, L.4    Erdjument-Bromage, H.5    Kumar, J.6    Tempst, P.7    Sif, S.8
  • 24
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • A. Frankel, N. Yadav, J. Lee, T.L. Branscombe, S. Clarke, and M.T. Bedford The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity J. Biol. Chem. 277 2002 3537 3543
    • (2002) J. Biol. Chem. , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 25
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • T.B. Miranda, M. Miranda, A. Frankel, and S. Clarke PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity J. Biol. Chem. 279 2004 22902 22907
    • (2004) J. Biol. Chem. , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 26
    • 0037224585 scopus 로고    scopus 로고
    • Identification of new drug sensitivity genes using genetic suppressor elements: Protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents
    • L. Gros, C. Delaporte, S. Frey, J. Decesse, B.R. de Saint-Vincent, L. Cavarec, A. Dubart, A.V. Gudkov, and A. Jacquemin-Sablon Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents Cancer Res. 63 2003 164 171
    • (2003) Cancer Res. , vol.63 , pp. 164-171
    • Gros, L.1    Delaporte, C.2    Frey, S.3    Decesse, J.4    De Saint-Vincent, B.R.5    Cavarec, L.6    Dubart, A.7    Gudkov, A.V.8    Jacquemin-Sablon, A.9
  • 28
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
    • J. Lee, J. Sayegh, J. Daniel, S. Clarke, and M.T. Bedford PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family J. Biol. Chem. 280 2005 32890 32896
    • (2005) J. Biol. Chem. , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 29
    • 0029773758 scopus 로고    scopus 로고
    • Modification of vectors pEF-BOS, pcDNA1, and pcDNA3 result in improved convenience and expression
    • L.A. Goldman, E.C. Cutrone, S.V. Kotenko, C.D. Krause, and J.A. Langer Modification of vectors pEF-BOS, pcDNA1, and pcDNA3 result in improved convenience and expression BioTechniques 21 1996 1013 1015
    • (1996) BioTechniques , vol.21 , pp. 1013-1015
    • Goldman, L.A.1    Cutrone, E.C.2    Kotenko, S.V.3    Krause, C.D.4    Langer, J.A.5
  • 30
    • 0015523314 scopus 로고
    • Studies on transfer ribonucleic acid-ribosome complexes. XIX. Effect of antibiotics on peptidyl puromycin synthesis on polyribosoms from Escherichia coli
    • S. Pestka Studies on transfer ribonucleic acid-ribosome complexes. XIX. Effect of antibiotics on peptidyl puromycin synthesis on polyribosoms from Escherichia coli J. Biol. Chem. 247 1972 4669 4678
    • (1972) J. Biol. Chem. , vol.247 , pp. 4669-4678
    • Pestka, S.1
  • 31
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain β propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins
    • H. Jing, J. Takagi, J.H. Liu, S. Lindgren, R.G. Zhang, A. Joachimiak, J.H. Wang, and T.A. Springer Archaeal surface layer proteins contain β propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins Structure (Camb.) 10 2002 1453 1464
    • (2002) Structure (Camb.) , vol.10 , pp. 1453-1464
    • Jing, H.1    Takagi, J.2    Liu, J.H.3    Lindgren, S.4    Zhang, R.G.5    Joachimiak, A.6    Wang, J.H.7    Springer, T.A.8
  • 33
    • 0036298629 scopus 로고    scopus 로고
    • Crystal structure of guanidinoacetate methyltransferase from rat liver: A model structure of protein arginine methyltransferase
    • J. Komoto, Y. Huang, Y. Takata, T. Yamada, K. Konishi, H. Ogawa, T. Gomi, M. Fujioka, and F. Takusagawa Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase J. Mol. Biol. 320 2002 223 235
    • (2002) J. Mol. Biol. , vol.320 , pp. 223-235
    • Komoto, J.1    Huang, Y.2    Takata, Y.3    Yamada, T.4    Konishi, K.5    Ogawa, H.6    Gomi, T.7    Fujioka, M.8    Takusagawa, F.9
  • 34
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • X. Zhang, and X. Cheng Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides Structure (Camb.) 11 2003 509 520
    • (2003) Structure (Camb.) , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 37
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • T. Cardozo, and M. Pagano The SCF ubiquitin ligase: insights into a molecular machine Nat. Rev. Mol. Cell Biol. 5 2004 739 751
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 39
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • R.M. Kagan, and S. Clarke Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes Arch. Biochem. Biophys. 310 1994 417 427
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.