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Volumn 585, Issue 17, 2011, Pages 2627-2634

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize, N-methylate and transfer long chain polyamines in diatoms

Author keywords

Aminopropyltransferase; Biosilica glass; Diatom; Long chain polyamine biosynthesis; N methylation

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE; ALGAL PROTEIN; HISTONE METHYLTRANSFERASE; LONG CHAIN POLYAMINE; POLYAMINE; SILAFFIN PROTEIN; SPERMIDINE SYNTHASE; UNCLASSIFIED DRUG;

EID: 80052187376     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.07.038     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 66149107356 scopus 로고    scopus 로고
    • The life of diatoms in the world's oceans
    • E.V. Armbrust The life of diatoms in the world's oceans Nature 459 2009 185 192
    • (2009) Nature , vol.459 , pp. 185-192
    • Armbrust, E.V.1
  • 2
    • 36148995460 scopus 로고    scopus 로고
    • A code for lysine modifications of a silica biomineralizing silaffin protein
    • DOI 10.1002/anie.200702413
    • M. Sumper, R. Hett, G. Lehmann, and S. Wenzl A code for lysine modifications of a silica biomineralizing silaffin protein Angew. Chem. Int. Ed. Engl. 46 2007 8405 8408 (Pubitemid 350114949)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.44 , pp. 8405-8408
    • Sumper, M.1    Hett, R.2    Lehmann, G.3    Wenzl, S.4
  • 3
    • 0037814710 scopus 로고    scopus 로고
    • Polycationic peptides from diatom biosilica that direct silica nanosphere formation
    • N. Kroger, R. Deutzmann, and M. Sumper Polycationic peptides from diatom biosilica that direct silica nanosphere formation Science 286 1999 1129 1132
    • (1999) Science , vol.286 , pp. 1129-1132
    • Kroger, N.1    Deutzmann, R.2    Sumper, M.3
  • 4
    • 0037131421 scopus 로고    scopus 로고
    • Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis
    • DOI 10.1126/science.1076221
    • N. Kroger, S. Lorenz, E. Brunner, and M. Sumper Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis Science 298 2002 584 586 (Pubitemid 35215309)
    • (2002) Science , vol.298 , Issue.5593 , pp. 584-586
    • Kroger, N.1    Lorenz, S.2    Brunner, E.3    Sumper, M.4
  • 5
    • 5644278803 scopus 로고    scopus 로고
    • Silica morphogenesis by alternative processing of silaffins in the diatom Thalassiosira pseudonana
    • DOI 10.1074/jbc.M407734200
    • N. Poulsen, and N. Kroger Silica morphogenesis by alternative processing of silaffins in the diatom Thalassiosira pseudonana J. Biol. Chem. 279 2004 42993 42999 (Pubitemid 39372192)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 42993-42999
    • Poulsen, N.1    Kroger, N.2
  • 6
    • 0033792083 scopus 로고    scopus 로고
    • Pleuralins are involved in theca differentiation in the diatom Cylindrotheca fusiformis
    • N. Kroger, and R. Wetherbee Pleuralins are involved in theca differentiation in the diatom Cylindrotheca fusiformis Protist 151 2000 263 273
    • (2000) Protist , vol.151 , pp. 263-273
    • Kroger, N.1    Wetherbee, R.2
  • 7
    • 21244480579 scopus 로고    scopus 로고
    • Biomineralization in diatoms: Characterization of novel polyamines associated with silica
    • DOI 10.1016/j.febslet.2005.06.001, PII S0014579305006940
    • M. Sumper, E. Brunner, and G. Lehmann Biomineralization in diatoms:characterization of novel polyamines associated with silica FEBS Lett. 579 2005 3765 3769 (Pubitemid 40897722)
    • (2005) FEBS Letters , vol.579 , Issue.17 , pp. 3765-3769
    • Sumper, M.1    Brunner, E.2    Lehmann, G.3
  • 8
    • 33748558453 scopus 로고    scopus 로고
    • Silica pattern formation in diatoms: Species-specific polyamine biosynthesis
    • DOI 10.1002/cbic.200600184
    • M. Sumper, and G. Lehmann Silica pattern formation in diatoms: species-specific polyamine biosynthesis Chembiochem 7 2006 1419 1427 (Pubitemid 44369094)
    • (2006) ChemBioChem , vol.7 , Issue.9 , pp. 1419-1427
    • Sumper, M.1    Lehmann, G.2
  • 9
    • 0242551242 scopus 로고    scopus 로고
    • Biomimetic Control of Size in the Polyamine-Directed Formation of Silica Nanospheres
    • DOI 10.1002/anie.200352212
    • M. Sumper, S. Lorenz, and E. Brunner Biomimetic control of size in the polyamine-directed formation of silica nanospheres Angew. Chem. Int. Ed. Engl. 42 2003 5192 5195 (Pubitemid 37411814)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.42 , pp. 5192-5195
    • Sumper, M.1    Lorenz, S.2    Brunner, E.3
  • 10
    • 0037192497 scopus 로고    scopus 로고
    • A phase separation model for the nanopatterning of diatom biosilica
    • DOI 10.1126/science.1070026
    • M. Sumper A phase separation model for the nanopatterning of diatom biosilica Science 295 2002 2430 2433 (Pubitemid 34270252)
    • (2002) Science , vol.295 , Issue.5564 , pp. 2430-2433
    • Sumper, M.1
  • 11
    • 79952748080 scopus 로고    scopus 로고
    • Nanopatterned protein microrings from a diatom that direct silica morphogenesis
    • A. Scheffel, N. Poulsen, S. Shian, and N. Kroger Nanopatterned protein microrings from a diatom that direct silica morphogenesis Proc. Natl. Acad. Sci. USA 108 2011 3175 3180
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3175-3180
    • Scheffel, A.1    Poulsen, N.2    Shian, S.3    Kroger, N.4
  • 13
    • 49249088143 scopus 로고    scopus 로고
    • Silica biomineralization in diatoms: The model organism Thalassiosira pseudonana
    • M. Sumper, and E. Brunner Silica biomineralization in diatoms: the model organism Thalassiosira pseudonana Chembiochem 9 2008 1187 1194
    • (2008) Chembiochem , vol.9 , pp. 1187-1194
    • Sumper, M.1    Brunner, E.2
  • 14
    • 77449159833 scopus 로고    scopus 로고
    • S-Adenosylmethionine decarboxylase
    • A.E. Pegg S-Adenosylmethionine decarboxylase Essays Biochem. 46 2009 25 45
    • (2009) Essays Biochem. , vol.46 , pp. 25-45
    • Pegg, A.E.1
  • 17
    • 34250171745 scopus 로고    scopus 로고
    • Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine
    • DOI 10.1016/j.febslet.2007.05.074, PII S0014579307006126
    • J.M. Knott, P. Romer, and M. Sumper Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine FEBS Lett. 581 2007 3081 3086 (Pubitemid 46899055)
    • (2007) FEBS Letters , vol.581 , Issue.16 , pp. 3081-3086
    • Knott, J.M.1    Romer, P.2    Sumper, M.3
  • 18
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • DOI 10.1074/jbc.R500031200
    • A.E. Pegg Regulation of ornithine decarboxylase J. Biol. Chem. 281 2006 14529 14532 (Pubitemid 43855154)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14529-14532
    • Pegg, A.E.1
  • 20
    • 77449090048 scopus 로고    scopus 로고
    • Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor
    • C. Kahana Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor Essays Biochem. 46 2009 47 61
    • (2009) Essays Biochem. , vol.46 , pp. 47-61
    • Kahana, C.1
  • 21
    • 77449136427 scopus 로고    scopus 로고
    • A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation
    • I.P. Ivanov, J.F. Atkins, and A.J. Michael A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation Nucleic Acids Res. 38 2010 353 359
    • (2010) Nucleic Acids Res. , vol.38 , pp. 353-359
    • Ivanov, I.P.1    Atkins, J.F.2    Michael, A.J.3
  • 22
    • 34848893660 scopus 로고    scopus 로고
    • Phylogenetic diversity and the structural basis of substrate specificity in the β/α-barrel fold basic amino acid decarboxylases
    • DOI 10.1074/jbc.M704066200
    • J. Lee, A.J. Michael, D. Martynowski, E.J. Goldsmith, and M.A. Phillips diversity and the structural basis of substrate specificity in the beta/alpha-barrel fold basic amino acid decarboxylases J. Biol. Chem. 282 2007 27115 27125 (Pubitemid 47501929)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 27115-27125
    • Lee, J.1    Michael, A.J.2    Martynowski, D.3    Goldsmith, E.J.4    Phillips, M.A.5
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 25
    • 67650815445 scopus 로고    scopus 로고
    • Antizyme and antizyme inhibitor, a regulatory tango
    • C. Kahana Antizyme and antizyme inhibitor, a regulatory tango Cell Mol. Life Sci. 66 2009 2479 2488
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 2479-2488
    • Kahana, C.1
  • 26
    • 57349131678 scopus 로고    scopus 로고
    • Investigations about N-aminopropyl transferases probably involved in biomineralization
    • P. Romer, A. Faltermeier, V. Mertins, T. Gedrange, R. Mai, and P. Proff Investigations about N-aminopropyl transferases probably involved in biomineralization J. Physiol. Pharmacol. 59 Suppl 5 2008 27 37
    • (2008) J. Physiol. Pharmacol. , vol.595 , Issue.SUPPL. , pp. 27-37
    • Romer, P.1    Faltermeier, A.2    Mertins, V.3    Gedrange, T.4    Mai, R.5    Proff, P.6
  • 27
    • 77953042159 scopus 로고    scopus 로고
    • Structural biology of S-adenosylmethionine decarboxylase
    • S. Bale, and S.E. Ealick Structural biology of S-adenosylmethionine decarboxylase Amino Acids 38 2010 451 460
    • (2010) Amino Acids , vol.38 , pp. 451-460
    • Bale, S.1    Ealick, S.E.2
  • 28
    • 80051572800 scopus 로고    scopus 로고
    • Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysing de novo diamine to triamine formation
    • doi:10.1111/j.1365-2958.2011.07757.x
    • R. Green, C.C. Hanfrey, K.A. Elliott, D.E. McCloskey, X. Wang, S. Kanugula, A.E. Pegg and A.J. Michael (2011). Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysing de novo diamine to triamine formation, Mol. Microbiol. doi:10.1111/j.1365-2958.2011.07757.x.
    • (2011) Mol. Microbiol
    • Green, R.1    Hanfrey, C.C.2    Elliott, K.A.3    McCloskey, D.E.4    Wang, X.5    Kanugula, S.6    Pegg, A.E.7    Michael, A.J.8
  • 29
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • S.C. Dillon, X. Zhang, R.C. Trievel, and X. Cheng The SET-domain protein superfamily: protein lysine methyltransferases Genome Biol. 6 2005 227
    • (2005) Genome Biol. , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 30
    • 33845487512 scopus 로고    scopus 로고
    • SET domain protein lysine methyltransferases: Structure, specificity and catalysis
    • DOI 10.1007/s00018-006-6274-5
    • C. Qian, and M.M. Zhou SET domain protein lysine methyltransferases: Structure,specificity and catalysis Cell Mol. Life Sci. 63 2006 2755 2763 (Pubitemid 44913316)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.23 , pp. 2755-2763
    • Qian, C.1    Zhou, M.-M.2
  • 31
    • 0037020195 scopus 로고    scopus 로고
    • Structures of SET domain proteins: Protein lysine methyltransferases make their mark
    • T.O. Yeates Structures of SET domain proteins: protein lysine methyltransferases make their mark Cell 111 2002 5 7
    • (2002) Cell , vol.111 , pp. 5-7
    • Yeates, T.O.1
  • 32
    • 0035854733 scopus 로고    scopus 로고
    • Silica-precipitating peptides from diatoms. The chemical structure of silaffin-A from Cylindrotheca fusiformis
    • N. Kroger, R. Deutzmann, and M. Sumper Silica-precipitating peptides from diatoms. The chemical structure of silaffin-A from Cylindrotheca fusiformis J. Biol. Chem. 276 2001 26066 26070
    • (2001) J. Biol. Chem. , vol.276 , pp. 26066-26070
    • Kroger, N.1    Deutzmann, R.2    Sumper, M.3
  • 33
    • 47049102867 scopus 로고    scopus 로고
    • Crystal structure of human spermine synthase: Implications of substrate binding and catalytic mechanism
    • H. Wu Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism J. Biol. Chem. 283 2008 16135 16146
    • (2008) J. Biol. Chem. , vol.283 , pp. 16135-16146
    • Wu, H.1
  • 34
    • 77957849604 scopus 로고    scopus 로고
    • Tudor domain
    • P. Lasko Tudor domain Curr. Biol. 20 2010 R666 R667
    • (2010) Curr. Biol. , vol.20
    • Lasko, P.1
  • 35
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Y. Shi, F. Lan, C. Matson, P. Mulligan, J.R. Whetstine, P.A. Cole, and R.A. Casero Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 Cell 119 2004 941 953 (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 36
    • 0033593052 scopus 로고    scopus 로고
    • Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase
    • DOI 10.1073/pnas.96.26.14777
    • D. Ober, and T. Hartmann Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase Proc. Natl. Acad. Sci. USA 96 1999 14777 14782 (Pubitemid 30019716)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.26 , pp. 14777-14782
    • Ober, D.1    Hartmann, T.2
  • 37
    • 0035808250 scopus 로고    scopus 로고
    • FAD-containing polyamine oxidases: A timely challenge for researchers in biochemistry and physiology of plants
    • DOI 10.1016/S0168-9452(00)00380-0, PII S0168945200003800
    • M. Sebela, A. Radova, R. Angelini, P. Tavladoraki, I.I. Frebort, and P. Pec FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants Plant Sci. 160 2001 197 207 (Pubitemid 32109929)
    • (2001) Plant Science , vol.160 , Issue.2 , pp. 197-207
    • Sebela, M.1    Radova, A.2    Angelini, R.3    Tavladoraki, P.4    Frebort, I.5    Pec, P.6
  • 38
    • 0029665630 scopus 로고    scopus 로고
    • 8-acetyltransferase involved in the pathway of 1,3-diaminopropane production in Acanthamoeba culbertsoni
    • DOI 10.1007/s004360050110
    • O.P. Shukla, S.O. Aisien, B. Bergmann, C. Hellmund, and R.D. Walter Identification of the polyamine N8-acetyltransferase involved in the pathway of 1,3-diaminopropane production in Acanthamoeba culbertsoni Parasitol. Res. 82 1996 270 272 (Pubitemid 26093111)
    • (1996) Parasitology Research , vol.82 , Issue.3 , pp. 270-272
    • Shukla, O.P.1    Aisien, S.O.2    Bergmann, B.3    Hellmund, C.4    Walter, R.D.5
  • 39
    • 77449131884 scopus 로고    scopus 로고
    • Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5′-methylthioadenosine
    • E. Albers Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5′- methylthioadenosine IUBMB Life 61 2009 113242
    • (2009) IUBMB Life , vol.61 , pp. 113242
    • Albers, E.1
  • 40
    • 67650511674 scopus 로고    scopus 로고
    • Multiple horizontal gene transfer events and domain fusions have created novel regulatory and metabolic networks in the oomycete genome
    • P.F. Morris, L.R. Schlosser, K.D. Onasch, T. Wittenschlaeger, R. Austin, and N. Provart Multiple horizontal gene transfer events and domain fusions have created novel regulatory and metabolic networks in the oomycete genome PLoS One 4 2009 e6133
    • (2009) PLoS One , vol.4 , pp. 6133
    • Morris, P.F.1    Schlosser, L.R.2    Onasch, K.D.3    Wittenschlaeger, T.4    Austin, R.5    Provart, N.6
  • 41
    • 34948896934 scopus 로고    scopus 로고
    • Long-Chain Polyamines (LCPAs) from marine sponge: Possible implication in spicule formation
    • DOI 10.1002/cbic.200700305
    • S. Matsunaga, R. Sakai, M. Jimbo, and H. Kamiya Long-chain polyamines (LCPAs) from marine sponge: possible implication in spicule formation Chembiochem 8 2007 1729 1735 (Pubitemid 47523677)
    • (2007) ChemBioChem , vol.8 , Issue.14 , pp. 1729-1735
    • Matsunaga, S.1    Sakai, R.2    Jimbo, M.3    Kamiya, H.4


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