جۆری توێژینه‌وه‌ : Original Article

نوسه‌ران

1 1Department of Biology, College of Education, University of Garmian, Kalar, KRG/Iraq

2 School of Biological Sciences, University of Reading, Reading, Berkshire, UK

پوخته‌

2-oxoglutarate-dependent (2-OG) dioxygenases [2(OG)-dioxygenases] are distributed in a wide
range of prokaryotes and eukaryotes, and are involved in many different important biological
activities, for example biosynthesis of plant products including plant hormones and antioxidants,
posttranslational modification, DNA/RNA damage repair and in certain organisms modulations
of epigenetic modifications. These 2(OG) dioxygenase enzymes contain a characteristic iron (Fe)-
binding active site. To understand their role in modulating mechanisms against unfavourable
conditions, the present study examined nuclear localization signal (NLS), genetic status,
phenotypic patterns of 14 T-DNA mutants of Arabidopsis containing an insert in their (2-OG)
dioxygenase genes. Results showed that predicted localizations of proteins encoded by
respective genes varied according to four different methods used in this analysis; seven, three,
one and one of them were predicted to be located in the nucleus according to the four methods,
respectively. Moreover, genotypic analysis confirmed the homozygosity of plant(s) of nine of
these mutant lines [N671573 (insert in At1g20270), N668172 (At1g68080), N652869
(At2g17720), N679576 (At3g06290), N678627 (At3g28490), N338446 (At4g35810), N683883
(At4g35820), N666896 (At5g18900), N598611 (At5g66060)] and phenotypic analysis including
vegetative, siliques and seed characteristics of those plants showed different characteristics
either within each mutant (homozygous and heterozygous), or between mutants and the WT.

Aik, W., McDonough, M.A., Thalhammer, A., Chowdhury, R. and Schofield, C.J. (2012) Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases. Current Opinion in Structural Biology22, 691-700.
Alberts, B., Johnson, A., Lewis, J., Martin, R., Roberts, K. and Watson, J. (2008) Molecular Biology of the Cell. 5th ed: Garland Science. New York: USA.
Chen, Z.J. and Tian, L. (2007) Roles of dynamic and reversible histone acetylation in plant development and polyploidy. Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression1769, 295-307.
Cheynier, V., Comte, G., Davies, K.M., Lattanzio, V. and Martens, S. (2013) Plant phenolics: recent advances on their biosynthesis, genetics, and ecophysiology. Plant Physiology and Biochemistry72, 1-20.
Cheynier, V., Comte, G., Davies, K.M., Lattanzio, V. and Martens, S. (2013) Plant phenolics: recent advances on their biosynthesis, genetics, and ecophysiology. Plant Physiology and Biochemistry72, 1-20.
Etchegaray, J.-P., Chavez, L., Huang, Y., Ross, K.N., Choi, J., Martinez-Pastor, B., Walsh, R.M., Sommer, C.A., Lienhard, M. and Gladden, A. (2015) The histone deacetylase SIRT6 controls embryonic stem cell fate via TET-mediated production of 5-hydroxymethylcytosine. Nature Cell Biology17, 545-557
Geilen, K. and Böhmer, M. (2015) Dynamic subnuclear relocalisation of WRKY40 in response to Abscisic acid in Arabidopsis thaliana.Nature Scientific Reports5.
Grandperret, V., NicolasFrancés, V., Wendehenne, D. and Bourque, S. (2014) Type‐II histone deacetylases: elusive plant nuclear signal transducers. Plant, Cell & Environment37, 1259-1269.
Hausinger, R.P. (2015) Biochemical diversity of 2-oxoglutarate-dependent oxygenases. in 2-Oxoglutarate-Dependent Oxygenases (Hausinger, R. P., and Schofield, C. J. eds.): Cambridge, UK: The Royal Society of Chemistry. 1-58.
Hewitson, K., Granatino, N., Welford, R., McDonough, M. and Schofield, C. (2005) Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling. Philosophical Transactions of the Royal Society of London A: Mathematical, Physical and Engineering Sciences363, 807-828.
Hewitson, K., Granatino, N., Welford, R., McDonough, M. and Schofield, C. (2005) Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling. Philosophical Transactions of the Royal Society of London A: Mathematical, Physical and Engineering Sciences363, 807-828.
Jans, D.A., Xiao, C.Y. and Lam, M.H. (2000) Nuclear targeting signal recognition: a key control point in nuclear transport? Bioessays22, 532-544.
Kobayashi, T. and Nishizawa, N.K. (2012) Iron uptake, translocation, and regulation in higher plants. Annual Review of Plant Biology63, 131-152.
Lange, A., Mills, R.E., Lange, C.J., Stewart, M., Devine, S.E. and Corbett, A.H. (2007) Classical nuclear localization signals: definition, function, and interaction with importin α. Journal of Biological Chemistry282, 5101-5105.
Lee, S., Doxey, A.C., McConkey, B.J. and Moffatt, B.A. (2012) Nuclear targeting of methyl-recycling enzymes in Arabidopsis thaliana is mediated by specific protein interactions. Molecular Plant5, 231-248.
Martens, S., Preuß, A. and Matern, U. (2010) Multifunctional flavonoid dioxygenases: Flavonol and anthocyanin biosynthesis in Arabidopsis thaliana L. Phytochemistry71, 1040-1049.
Saito, K., Yonekura-Sakakibara, K., Nakabayashi, R., Higashi, Y., Yamazaki, M., Tohge, T. and Fernie, A.R. (2013) The flavonoid biosynthetic pathway in Arabidopsis: structural and genetic diversity. Plant Physiology and Biochemistry72, 21-34.
Uji, T., Takahashi, M., Saga, N. and Mikami, K. (2010) Visualization of nuclear localization of tranion factors with cyan and green fluorescent proteins in the red alga Porphyra yezoensisMarine Biotechnology12, 150-159.
Wang, J., Yu, Y., Zhang, Z., Quan, R., Zhang, H., Ma, L., Deng, X.W. and Huang, R. (2013) Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid synthesis. The Plant Cell25, 625-636