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Wasternack, C. (13)Feussner, I. (11)Porzel, A. (11)Adam, G. (8)Brandt, W. (6)Schmidt, J. (6)Strack, D. (6)Hause, B. (5)Miersch, O. (5)Parthier, B. (5)Sung, T. V. (5)Fengler, A. (4)Kramell, R. (4)Ripperger, H. (4)Ansorge, S. (3)Faust, J. (3)Kühn, H. (3)Neubert, K. (3)Reinhold, D. (3)Scheel, D. (3)Wrenger, S. (3)Apel, K. (2)Beale, M. (2)Bohlmann, H. (2)Boland, W. (2)Kohlmann, M. (2)Kutchan, T. M. (2)Lien, T. P. (2)Schliemann, W. (2)Schmidt, A. (2)Schneider, B. (2)Schröder, G. (2)Schröder, J. (2)Vignutelli, A. (2)Bachmann, A. (1)Balkenhohl, T. (1)Bardshiri, E. (1)Berger, T. (1)Binarová, P. (1)Blée, E. (1)Bruhn, C. (1)Böhm, A. (1)Börner, T. (1)Chou, W. (1)Churin, J. (1)Clemens, S. (1)Doležel, J. (1)Dráber, P. (1)Eckermann, S. (1)Edrada, R. A. (1)Elomaa, P. (1)Feussner, K. (1)Gerisch, M. (1)Graner, A. (1)Greulich, F. (1)Griehl, C. (1)Helariutta, Y. (1)Hilpert, B. (1)Hoffmann, F. (1)Kilpeläinen, I. (1)Knöfel, H.-D. (1)Kolbe, A. (1)Kotilainen, M. (1)Krumm, T. (1)Kuntzsch, A. (1)Lee, J. (1)Löbler, M. (1)Maier, W. (1)Maucher, H. P. (1)Menezes, A. S. (1)Merzweiler, K. (1)Moreira, J. J. (1)Morel, A. F. (1)Nennstiel, D. (1)Nürnberger, T. (1)Ortel, B. (1)Pauli, H. H. (1)Phuong, N. M. (1)Plass, M. (1)Proksch, P. (1)Quan, T. D. (1)Raiber, S. (1)Ratajczak, R. (1)Rousset, C. (1)Schneider, G. (1)Schroeder, J. I. (1)Simpson, T. J. (1)Sinks, U. (1)Sontag, B. (1)Steinborn, D. (1)Steiner, U. (1)Teeri, T. H. (1)
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Publikation
We found three methyl jasmonate−induced lipoxygenases with molecular masses of 92 kDa, 98 kDa, and 100 kDa (LOX‐92, ‐98 and ‐100) [Feussner, I., Hause, B., Vörös, K., Parthier, B. & Wasternack, C. (1995) Plant J. 7 , 949−957]. At least two of them (LOX‐92 and LOX‐100), were shown to be localized within chloroplasts of barley leaves. Here, we describe the isolation of a cDNA (3073 bp) coding for LOX‐100, a protein of 936 amino acid residues and a molecular mass of 106 kDa. By sequence comparison this lipoxygenase could be identified as LOX2‐type lipoxygenase and was therefore designated LOX2 : Hv : 1 . The recombinant lipoxygenase was expressed in Escherichia coli and characterized as linoleate 13‐LOX and arachidonate 15‐LOX, respectively. The enzyme exhibited a pH optimum around pH 7.0 and a moderate substrate preference for linoleic acid. The gene was transiently expressed after exogenous application of jasmonic acid methyl ester with a maximum between 12 h and 18 h. Its expression was not affected by exogenous application of abscisic acid. Also a rise of endogenous jasmonic acid resulting from sorbitol stress did not induce LOX2 : Hv : 1 , suggesting a separate signalling pathway compared with other jasmonate‐induced proteins of barley. The properties of LOX2 : Hv : 1 are discussed in relation to its possible involvement in jasmonic acid biosynthesis and other LOX forms of barley identified so far.