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Eukaryotic Cell, March 2009, p. 296-305, Vol. 8, No. 3
1535-9778/09/$08.00+0     doi:10.1128/EC.00197-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Disruption of the Aopex11-1 Gene Involved in Peroxisome Proliferation Leads to Impaired Woronin Body Formation in Aspergillus oryzae ^,

Cristopher Salazar Escaño,^1, Praveen Rao Juvvadi,^1,, Feng Jie Jin,² Tadashi Takahashi,² Yasuji Koyama,² Shuichi Yamashita,³ Jun-ichi Maruyama,¹ and Katsuhiko Kitamoto^1*

Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan,¹ Noda Institute of Scientific Research, 399 Noda, Noda-shi, Chiba 278-0037, Japan,² Department of Agricultural and Environmental Biology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan³

Received 16 June 2008/ Accepted 30 December 2008

The Woronin body, a unique organelle found in the Pezizomycotina, plugs the septal pore upon hyphal damage to prevent excessive cytoplasmic bleeding. Although it was previously shown that the Woronin body buds out from the peroxisome, the relationship between peroxisomal proliferation/division and Woronin body differentiation has not been extensively investigated. In this report, we examined whether Pex11 required for peroxisomal proliferation participates in Woronin body formation in Aspergillus oryzae. A. oryzae contained two orthologous PEX11 genes that were designated Aopex11-1 and Aopex11-2. Deletion of Aopex11 genes revealed that only the Aopex11-1 strain showed reduced growth and enlarged peroxisomes in the presence of oleic acid as a sole carbon source, indicating a defect in peroxisomal function and proliferation. Disruption of Aopex11-1 gene impaired the Woronin body function, leading to excessive loss of the cytosol upon hyphal injury. Dual localization analysis of the peroxisome and Woronin body protein AoHex1 demonstrated that Woronin bodies fail to fully differentiate from peroxisomes in the Aopex11-1 strain. Furthermore, distribution of AoHex1 was found to be peripheral in the enlarged peroxisome or junctional in dumbbell-shaped peroxisomes. Electron microscopy of the Aopex11-1 strain revealed the presence of Woronin bodies that remained associated with organelles resembling peroxisomes, which was supported from the sucrose gradient centrifugation confirming that the Woronin body protein AoHex1 overlapped with the density-shifted peroxisome in the Aopex11-1 strain. In conclusion, the present study describes the role of Pex11 in Woronin body differentiation for the first time.

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* Corresponding author. Mailing address: Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81 3 5841 5161. Fax: 81 3 5841 8033. E-mail: akitamo{at}mail.ecc.u-tokyo.ac.jp

Published ahead of print on 9 January 2009.

Supplemental material for this article may be found at http://ec.asm.org/.

C.S.E. and P.R.J. contributed equally to this work.

Present address: Center for Microbial Pathogenesis, Duke Mycology Research Unit, Duke University Medical Center, Durham, NC 27710.

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Eukaryotic Cell, March 2009, p. 296-305, Vol. 8, No. 3
1535-9778/09/$08.00+0     doi:10.1128/EC.00197-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.