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Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity

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Abstract

O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs.

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Abbreviations

4-CL:

4-Coumaoryl-CoA ligase

COMT:

Caffeic acid OMT

CCoAOMT:

Caffeoyl coenzyme A OMT

MD:

Molecular dynamics simulations

OMT:

O-Methyltransferase

SAM:

S-Adenosy-l-methionine

References

  • Cho J-H, Park Y, Ahn J-H, Lim Y, Rhee S (2008) Structural and functional insights of O-methyltransferase from Bacillus cereus. J Mol Biol 382:987–997

    Article  CAS  PubMed  Google Scholar 

  • Dixon RA, Palva NC (1995) Stress-induced phenylpropanoid metabolism. Plant Cell 7:1085–1097

    Google Scholar 

  • Ferrer J-L, Zubieta C, Dixon RA, Noel JP (2005) Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase. Plant Physiol 137:1009–1017

    Article  CAS  PubMed  Google Scholar 

  • Fischbach R, Kossmann B, Panten H, Steinbrecher R, Heller W, Seidlitz HK, Sandermann H, Hertkorn N, Schnitzler JP (1999) Seasonal accumulation of ultraviolet-B screening pigments in needles of Norway spruce (Picea abies (L.) Karst.). Plant Cell Environ 22:27–37

    Article  CAS  Google Scholar 

  • Frick S, Kutchan TM (1999) Molecular cloning and functional expression of O-methyltransferases common to isoquinoline alkaloid and phenylpropanoid biosynthesis. Plant J 17:329–339

    Article  CAS  PubMed  Google Scholar 

  • Gauthier A, Gulick P, Ibrahim RK (1998) Characterization of two cDNA clones which encode O-methyltransferases for the methylation of both flavonoid and phenylpropanoid compounds. Arch Biochem Biophys 351:243–249

    Article  CAS  PubMed  Google Scholar 

  • Ibdah M, Zhang XH, Schmidt J, Vogt T (2003) A novel Mg+2 dependent O-methyltransferase in the phenylpropanoid metabolism of Mesembryanthemum crystallinum. J Biol Chem 278:43961–43972

    Article  CAS  PubMed  Google Scholar 

  • Ibrahim RK, Bruneau A, Bantignies B (1998) Plant O-methyltransferase: molecular analysis, common signature and classification. Plant Mol Biol 36:1–10

    Article  CAS  PubMed  Google Scholar 

  • Kim DH, Kim B-G, Lee Y, Ryu JY, Lim Y, Hur H-G, Ahn J-H (2005) Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli. J Biotechnol 138:155–162

    Article  Google Scholar 

  • Kim B-G, Lee YJ, Park Y, Lim Y, Ahn J-H (2006) Caffeic acid O-methyltransferase from Populus deltoids: functional expression and characterization. J Plant Biol 49:55–60

    Article  CAS  Google Scholar 

  • Kopycki JG, Rauh D, Chumanevich AA, Neumann P, Vogt T, Stubbs MT (2008a) Biochemical and structural analysis of substrate promiscuity in plant Mg2+-dependent O-methyltransferase. J Mol Biol 378:154–164

    Article  CAS  PubMed  Google Scholar 

  • Kopycki JG, Stubbs MT, Brandt W, Hagemann M, Porzel A, Schmidt J, Schliemann W, Zenk MH, Vogt T (2008b) Functional and structural characterization of a cation-dependent O-methyltransferase from the cyanobacterium Synechocystis sp. strain PCC 6803. J Biol Chem 283:20888–20896

    Article  CAS  PubMed  Google Scholar 

  • Lam KC, Irahim RK, Behdad B, Dayanandan S (2007) Structure, function, and evolution of plant O-methyltransferases. Genome 50:1001–1013

    Article  CAS  PubMed  Google Scholar 

  • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283–291

    Article  CAS  Google Scholar 

  • Lee YJ, Kim B-G, Park Y, Lim Y, Hur H-G, Ahn J-H (2006) Biotransformation of flavonoids with O-methyltransferase from Bacillus cereus. J Miocrobiol Biotechnol 16:1090–1096

    CAS  Google Scholar 

  • Lee YJ, Jeon Y, Lee JS, Kim B-G, Lee CH, Ahn J-H (2007) Enzymatic synthesis of phenolic CoAs using 4-coumarate:coenzyme A ligase (4CL) from rice. Bull Kor Chem Soc 28:365–366

    Article  CAS  Google Scholar 

  • Lee YJ, Kim B-G, Lim Y, Chenog Y, Ahn J-H (2008) Cation dependent O-methyltransferases from rice. Planta 227:641–647

    Article  CAS  PubMed  Google Scholar 

  • Liu C-J, Deavours BE, Richard SB, Ferrer J-L, Blount JW, Huhman D, Dixon RA, Noel JP (2006) Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18:3656–3669

    Article  CAS  PubMed  Google Scholar 

  • Moore RC, Purugganan MD (2005) The evolutionary dynamics of plant duplicate genes. Curr Opin Plant Biol 8:122–128

    Article  CAS  PubMed  Google Scholar 

  • Pan H, Lundgren LN (1995) Phenolic extractives from root bark of Picea abies. Phytochemistry 39:1423–1428

    Article  CAS  PubMed  Google Scholar 

  • Shi R, Sun Y-H, Li Q, Heber S, Sederoff R, Chiang VL (2010) Towards a system spproach for lignin biosynthesis in Populus trichocarpa: transcript abundance and specificity of the monolignol biosynthetic genes. Plant Cell Physiol 51:144–163

    Google Scholar 

  • Slimestad R (2003) Flavonoids in buds and young needles of Picea, Pinus and Abies. Biochem Syst Ecol 31:1247–1255

    Article  CAS  Google Scholar 

  • Tahara S (2007) A journey of twenty-five years through the ecological biochemistry of flavonoids. Biosci Biotechnol Biochem 71:1387–1404

    Article  CAS  PubMed  Google Scholar 

  • Vogt T (2004) Regioselectivity and kinetic properties of a plant natural product O-methyltransferase are determined by its N-terminal domain. FEBS Lett 561:159–162

    Article  CAS  PubMed  Google Scholar 

  • Wang J, Pichersky E (1999) Identification of specific residues involved in substrate discrimination in two plant O-methyltransferases. Arch Biochem Biophys 368:172–180

    Article  CAS  PubMed  Google Scholar 

  • Yang H, Ahn J-H, Jeong KJ, Lee S, Lim Y (2003) The homodimerization of Thalictrum tuberosum O-methyltransferases by homology-based modeling. Bull Kor Chem Soc 24:1–5

    CAS  Google Scholar 

  • Zhu BT, Ezell EL, Liehr JG (1994) Catechol-O-methyltransferase-catalyzed rapid O-methylation of mutagenic flavonoids. J Biol Chem 269:292–299

    CAS  PubMed  Google Scholar 

  • Zubieta C, He X-Z, Dixon RA, Noel JP (2001) Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferase. Nature Struct Biol 8:271–279

    Article  CAS  PubMed  Google Scholar 

  • Zubieta C, Kota P, Ferrer J-L, Dixon RA, Noel JP (2002) Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 14:1256–1277

    Article  Google Scholar 

Download references

Acknowledgments

This work was supported by a grant from the Biogreen 21 Program, Rural Development Administration, Republic of Korea, Korean Rural Development Administration, Agenda program (NIAS, 11-30-68) and also partially by Priority Research Centers Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2009-0093824).

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Authors and Affiliations

  1. Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, 143-701, Korea

    Bong-Gyu Kim, Dae Hwan Kim, Su Hyun Sung, Dong-Eun Kim, Youhoon Chong & Joong-Hoon Ahn

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  1. Bong-Gyu Kim
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  2. Dae Hwan Kim
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  3. Su Hyun Sung
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  4. Dong-Eun Kim
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  6. Joong-Hoon Ahn
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Correspondence to Joong-Hoon Ahn.

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B.-G. Kim and D. H. Kim contributed equally to this work.

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Kim, BG., Kim, D.H., Sung, S.H. et al. Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity. Planta 232, 837–844 (2010). https://doi.org/10.1007/s00425-010-1223-9

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  • DOI: https://doi.org/10.1007/s00425-010-1223-9

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