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Transcriptional and translational analyses of poplar anionic peroxidase isoenzymes
Journal of Wood Science volume 53, pages 427–435 (2007)
Abstract
Anionic peroxidases have been proposed to be a key enzyme for lignification in poplar. On the other hand, there are many genes encoding an anionic peroxidase in Populus trichocarpa genome, and their physiological functions are still unknown. Ampholine isoelectric focusing analysis revealed anionic peroxidases as dominant peroxidases in enzyme preparations from various organs. Using two-dimensional electrophoresis (2-DE) followed by peptide mass fingerprint (PMF) analysis, we surveyed the localization of anionic peroxidase isoenzymes in various organs of Populus alba L. Peroxidase isoenzymes were extracted from various organs and fractionated by a Concanavallin A Sepharose column. Each protein was separated by 2-DE gels and some anionic peroxidase isoenzymes in each organ were identified via PMF analysis. Transcript and protein of individual peroxidase indicate that the expression profile of each isoenzyme is quite different, for example, organspecific gene, stress-response gene, and multifunction gene, even though they are in the same cluster. These results suggest that individual anionic isoenzymes in this small cluster were differently regulated at transcription, translation, or posttranslation.
References
Lagrimini LM, Burkhart W, Moyer M, Rothstein S (1987) Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: molecular analysis and tissue-specific expression. Proc Natl Acad Sci USA 84:7542–7546
Blee KA, Choi JW, O’Connell AP, Schuch W, Lewis NG, Bolwell GP (2003) A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification. Phytochemistry 64:163–176
Li Y, Kajita S, Kawai S, Katayama Y, Morohoshi N (2003) Down-regulation of an anionic peroxidase in transgenic aspen and its effect on lignin characteristics. J Plant Res 116:175–182
Osakabe K, Koyama H, Kawai S, Katayama Y, Morohoshi N (1995) Molecular cloning of two tandemly arranged peroxidase genes from Populus kitakamiensis and their differential regulation in the stem. Plant Mol Biol 28:677–689
Christensen JH, Bauw G, Welinder KG, Van Montagu M, Boerjan W (1998) Purification and characterization of peroxidases correlated with lignification in poplar xylem. Plant Physiol 118:125–135
Christensen JH, Overney S, Rohde A, Diaz WA, Bauw G, Simon P, Van Montagu M, Boerjan W (2001) The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: cDNA isolation, characterization and expression. Plant Mol Biol 47:581–593
Tognolli M, Penel C, Greppin H, Simon P (2002) Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene 288:129–138
Passardi F, Longet D, Penel C, Dunand C (2004) The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochemistry 65:1879–1893
Tuskan GA, and 109 authors (2006) The genome of black cottonwood, Populus trichocarpa (Torr. & Gray). Science 313:1596–1604
Valerio L, De Meyer M, Penel C, Dunand C (2004) Expression analysis of the Arabidopsis peroxidase multigenic family. Phytochemistry 65:1331–1342
Welinder KG, Justesen AF, Kjaersgard IV, Jensen RB, Rasmussen SK, Jespersen HM, Duroux L (2002) Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana. Eur J Biochem 269:6063–6081
Aharoni A, Vorst O (2001) DNA microarrays for functional plant genomics. Plant Mol Biol 48:99–118
Gygi SP, Rochon Y, Franza BR, Aebersold R (1999) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19:1720–1730
Serino G, Deng XW (2003) The COP9 signalosome: regulating plant development through the control of proteolysis. Annu Rev Plant Biol 54:165–182
Sasaki S, Nishida T, Tsutsumi Y, Kondo R (2004) Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β-O-4 linkage. FEBS Lett 562:197–201
Sasaki K, Hiraga S, Ito H, Seo S, Matsui H, Ohashi Y (2002) Wound-inducible tobacco peroxidase gene expresses preferentially in the vascular system. Plant Cell Physiol 43:108–117
Nanjo T, Futamura N, Nishiguchi M, Igasaki T, Shinozaki K, Shinohara K (2004) Characterization of full-length enriched expressed sequence tags of stress-treated poplar leaves. Plant Cell Physiol 45:1738–1748
Tsutsumi Y, Sakai K (1994) Lignin biosynthesis in woody angiosperm tissues II. Peroxidase related to syringyl and guaiacyl lignin biosynthesis in Populus callus cultures. Mokuzai Gakkaishi 40: 744–750
Shimizu M, Yuda N, Nakamura T, Tanaka H, Wariishi H (2005) Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin. Proteomics 5:3919–3931
Rosenfeld J, Capdevielle J, Guillemot JC, Ferrara P (1992) In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis. Anal Biochem 203:173–179
Kato Y, Sakuma Y, Azuma T, Ando A, Miura K, Takabe K, Tamai Y (2001) Isolation and characterization of a novel anionic peroxidase cDNA found in poplar (Populus nigra) suspension cultured cells. J Wood Sci 47:165–170
Takeuchi M, Takabe K, Fujita M (2005) Immunolocalization of an anionic peroxidase in differentiating poplar xylem. J Wood Sci 51:317–322
Navazio L, Miuzzo M, Royle L, Baldan B, Varotto S, Merry AH, Harvey DJ, Dwek RA, Rudd PM, Mariani P (2002) Monitoring endoplasmic reticulum-to-Golgi traffic of a plant calreticulin by protein glycosylation analysis. Biochemistry 41:14141–14149
Bestwick CS, Brown IR, Mansfield JW (1998) Localized changes in peroxidase activity accompany hydrogen peroxide generation during the development of a nonhost hypersensitive reaction in lettuce. Plant Physiol 118:1067–1078
Bolwell GP, Butt VS, Davies DR, Zimmerlin A (1995) The origin of the oxidative burst in plants. Free Radical Res 23:517–532
Bradley DJ, Kjellbon P, Lamb CJ (1992) Elicitor-and woundinduced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defense response. Cell 70:21–30
Kawaoka A, Matsunaga E, Endo S, Kondo S, Yoshida K, Shinmyo A, Ebinuma H (2003) Ectopic expression of a horseradish peroxidase enhances growth rate and increases oxidative stress resistance in hybrid aspen. Plant Physiol 132:1177–1185
Kristensen BK, Bloch H, Rasmussen SK (1999) Barley coleoptile peroxidases. Purification, molecular cloning, and induction by pathogens. Plant Physiol 120:501–512
Showalter AM (1993) Structure and function of plant cell wall proteins. Plant Cell 5:9–23
Stoessl A (1967) The antifungal factors in barley. IV. Isolation, structure, and synthesis of the hordatines. Can J Chem 45: 1745–1760
Wojtaszek P (1997) Oxidative burst: an early plant response to pathogen infection. Biochem J 322:681–692
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Part of this study was presented at the 50th Lignin Symposium (Nagoya) and the 56th Annual Meeting of the Japan Wood Research Society (Akita)
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Sasaki, S., Shimizu, M., Wariishi, H. et al. Transcriptional and translational analyses of poplar anionic peroxidase isoenzymes. J Wood Sci 53, 427–435 (2007). https://doi.org/10.1007/s10086-007-0888-6
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DOI: https://doi.org/10.1007/s10086-007-0888-6