Isoform-specific subcellular localization of Zea mays lipoxygenases and oxo-phytodienoate reductase 2 Academic Article

abstract

• 2017 Plant 9- and 13-lipoxygenases (9- and 13-LOXs) function in an early step of the oxylipin biosynthesis pathway. Here we report diverse subcellular localization profiles of four maize LOX family proteins and one oxo-phytodienoate reductase 2, subcellular localization of which could not be predicted by bioinformatics tools. Fluorescent protein-tagged LOX proteins were transiently expressed in maize B73 protoplasts as well as in stably transformed Arabidopsis thaliana. Localization profiles of maize 9-LOXs were more diverse than that of reported 13-LOX isoforms and spanned cytoplasm, plastids and tonoplasts, suggesting compartmentation of different oxylipin production inside of the cells. Localization profiles of maize 9-LOX were mostly consistent between maize and Arabidopsis, suggesting subcellular targeting mechanisms of these isoforms are conserved between monocots and dicots.

authors

• Koiwa, Hisashi
• Kolomiets, Michael

published proceedings

• Plant Gene

author list (cited authors)

• Tolley, J. P., Nagashima, Y., Gorman, Z., Kolomiets, M. V., & Koiwa, H.

citation count

• 12

complete list of authors

• Tolley, Jordan P||Nagashima, Yukihiro||Gorman, Zachary||Kolomiets, Michael V||Koiwa, Hisashi

publication date

• March 2018

publisher

• Elsevier  Publisher

published in

• Plant gene  Journal

Digital Object Identifier (DOI)

• 10.1016/j.plgene.2017.12.002

start page

• 36

end page

• 41

volume

• 13

URL

• http://dx.doi.org/10.1016/j.plgene.2017.12.002