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Functional Plant Biology Functional Plant Biology Society
Plant function and evolutionary biology
RESEARCH ARTICLE

Soybean vegetative lipoxygenases are not vacuolar storage proteins

Glenn W. Turner A , Howard D. Grimes B and B. Markus Lange A C
+ Author Affiliations
- Author Affiliations

A Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

B School of Molecular Biosciences, Washington State University, Pullman, WA 99164-7520, USA.

C Corresponding author. Email: lange-m@wsu.edu

Functional Plant Biology 38(10) 778-787 https://doi.org/10.1071/FP11047
Submitted: 15 February 2011  Accepted: 23 July 2011   Published: 16 September 2011

Abstract

The paraveinal mesophyll (PVM) of soybean is a distinctive uniseriate layer of branched cells situated between the spongy and palisade chlorenchyma of leaves that contains an abundance of putative vegetative storage proteins, Vspα and Vspβ, in its vacuoles. Soybean vegetative lipoxygenases (five isozymes designated as Vlx(A–E)) have been reported to co-localise with Vsp in PVM vacuoles; however, conflicting results regarding the tissue-level and subcellular localisations of specific Vlx isozymes have been reported. We employed immuno-cytochemistry with affinity-purified, isozyme-specific antibodies to reinvestigate the subcellular locations of soybean Vlx isozymes during a sink limitation experiment. VlxB and VlxC were localised to the cytoplasm and nucleoplasm of PVM cells, whereas VlxD was present in the cytoplasm and nucleoplasm of mesophyll chlorenchyma (MC) cells. Label was not associated with storage vacuoles or any evident protein bodies, so our results cast doubt on the hypothesis that Vlx isozymes function as vegetative storage proteins.

Additional keywords: localisation, paraveinal mesophyll, vegetative lipoxygenase.


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