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JXB Advance Access published online on March 21, 2006
Journal of Experimental Botany, doi:10.1093/jxb/erj113
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© The Author [2006]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received September 1, 2005
Accepted January 10, 2006

RESEARCH PAPER

Subcellular localization of Strboh proteins and NADPH-dependent O2--generating activity in potato tuber tissues

Michie Kobayashi 1, Kazuhito Kawakita 1, Masayoshi Maeshima 2, Noriyuki Doke 1, and Hirofumi Yoshioka 3 *

1 Plant Pathology Laboratory, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan
2 Laboratory of Cell Dynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan
3 Laboratory of Defense in Plant-Pathogen Interactions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan

* To whom correspondence should be addressed.
Hirofumi Yoshioka, E-mail: hyoshiok{at}agr.nagoya-u.ac.jp


  Abstract

Rapid generation of reactive oxygen species (ROS) at the cell surface has been implicated in plant defence responses. Genetic evidence indicates that a plant NADPH oxidase (Rboh; respiratory burst oxidase homologue) is associated with oxidative burst. However, there is not enough physiological evidence of Rboh localization available yet. Isozyme-specific antibodies against potato StrbohA and StrbohB (St; Solanum tuberosum) were prepared to investigate the localization of these proteins. Immunoblot analyses using potato microsomal proteins revealed that StrbohA was expressed constitutively at a low level, whereas the accumulation of StrbohB protein was induced by the cell wall elicitor of the potato pathogen Phytophthora infestans. It is demonstrated here that StrbohA and StrbohB are distributed in plasma membrane fractions which have been separated by sucrose density-gradient centrifugation using their specific antibodies. Green fluorescent protein-tagged Strboh proteins were also located on the plasma membrane by transient expression assay in onion epidermal cells. Additionally, NADPH-dependent O2--generating activities in plasma membrane fractions were diphenylene iodonium-sensitive and NaN3-insensitive. These data suggest that StrbohA and StrbohB are predominantly localized on the plasma membrane and regulate ROS production in defence signalling.

Keywords: NADPH oxidase; Rboh; reactive oxygen species; subcellular localization.
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