Molecular characterization of L2 lipoxygenase from maize embryos

Molecular characterization of L2 lipoxygenase from maize embryos We investigated the expression and accumulation pattern of lipoxygenaseisoforms throughout the maize plant life. Two forms of lipoxygenase L1and L2 have been identified as acidic proteins of 100 kDa (pI 6.4) and90 kDa (pI 5.5-5.7) which accumulate in dry embryos and in variousorgans of maize seedlings. In young embryos, only the L2 form wasdetected and accumulation of L2 mRNA decreased during embryodevelopment. Identification of lipoxygenases from in vivo and in vitro synthesized proteins indicates that similar levels of both L1and L2 forms accumulated during treatment with abscisic acid, (ABA)gibberellic acid (GA3) and jasmonic acid (JA). However,differences in the activity of both enzymes were detected. By using anantiserum directed against purified L2 we isolated and characterized apartial cDNA clone of maize embryos encoding a lipoxygenase. The deducedamino acid sequence of L2 cDNA shares 78% identity with the rice L2protein, and 51-56% identity with lipoxygenases from thedicotyledonous plants soybean and Arabidopsis/. DNA blotanalysis indicated that maize contains a family of lipoxygenase geneswhich are presently being characterized. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Molecular characterization of L2 lipoxygenase from maize embryos

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005742719019
Publisher site
See Article on Publisher Site

Abstract

We investigated the expression and accumulation pattern of lipoxygenaseisoforms throughout the maize plant life. Two forms of lipoxygenase L1and L2 have been identified as acidic proteins of 100 kDa (pI 6.4) and90 kDa (pI 5.5-5.7) which accumulate in dry embryos and in variousorgans of maize seedlings. In young embryos, only the L2 form wasdetected and accumulation of L2 mRNA decreased during embryodevelopment. Identification of lipoxygenases from in vivo and in vitro synthesized proteins indicates that similar levels of both L1and L2 forms accumulated during treatment with abscisic acid, (ABA)gibberellic acid (GA3) and jasmonic acid (JA). However,differences in the activity of both enzymes were detected. By using anantiserum directed against purified L2 we isolated and characterized apartial cDNA clone of maize embryos encoding a lipoxygenase. The deducedamino acid sequence of L2 cDNA shares 78% identity with the rice L2protein, and 51-56% identity with lipoxygenases from thedicotyledonous plants soybean and Arabidopsis/. DNA blotanalysis indicated that maize contains a family of lipoxygenase geneswhich are presently being characterized.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 29, 2004

References

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