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Plant and Cell Physiology Advance Access published online on February 28, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn038
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Plant Catalase is Imported into Peroxisome by Pex5p but Distinct from Typical PTS1 Import.

Yoshimi Oshima1, Akane Kamigaki1,2, Chihiro Nakamori2, Shoji Mano2, Makoto Hayashi2, Mikio Nishimura2 and Muneharu Esaka1,*

1Graduate School of Biosphere Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, 739-8528 Japan
2Department of Cell Biology, National Institute for Basic Biology, Okazaki, 444-8585 Japan

*Corresponding author: Prof. Muneharu Esaka. Graduate School of Biosphere Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, 739-8528, Japan. Tel: +81-82-424-7927, Fax: +81-82-422-7067, E-mail: mesaka{at}hiroshima-u.ac.jp


  Abstract

We have previously demonstrated that the targeting signal of pumpkin catalase, Cat1, is an internal PTS1 (peroxisomal targeting signal 1)-like sequence, QKL, located at -13 to -11 from the C-terminus, which is different from the typical PTS1 SKL motif located in the C-terminus. Here we show that Cat1 import into peroxisome is dependent on cytosolic PTS receptor, Pex5p, in Arabidopsis similar to typical PTS1 import, and that other components for transport of peroxisomal matrix proteins such as Pex14p, Pex13p, Pex12p and Pex10p also contribute to the import of Cat1. Interestingly, however, we found that Cat1 interacts with the N-terminal domain of Pex5p, but not the C-terminal domain for interaction with the typical PTS1, revealing that Pex5p recognizes Cat1 in a manner distinct from typical PTS1.

Keywords: Arabidopsis - Catalase - Peroxisome - Peroxisomal targeting signal - PEX - two-hybrid system

(Received January 19, 2008; Accepted February 23, 2008)
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