TAILIEUCHUNG - Báo cáo khoa học: Dynamin-like protein-dependent formation of Woronin bodies in Saccharomyces cerevisiae upon heterologous expression of a single protein

Filamentous ascomycetes harbor Woronin bodies and glyoxysomes, two types of microbodies, within one cell at the same time. The dominant pro-tein of the Neurospora crassaWoronin body, HEX1, forms a hexagonal core crystal via oligomerization and evidence has accumulated that Woro-nin bodies bud off from glyoxysomes. | ễFEBS Journal Dynamin-like protein-dependent formation of Woronin bodies in Saccharomyces cerevisiae upon heterologous expression of a single protein Christian Wurtz Wolfgang Schliebs Ralf Erdmann and Hanspeter Rottensteiner Institut fur Physiologische Chemie Ruhr-Universitat Bochum Germany Keywords filamentous fungi Neurospora crassa peroxisome protein import yeast Correspondence H. Rottensteiner Institut fur Physiologische Chemie Abt. Systembiochemie Ruhr-Universitat Bochum D-44780 Bochum Germany Fax 49 234 321 4266 Tel 49 234 322 7046 E-mail Received 22 January 2008 revised 27 March 2008 accepted 2 April 2008 doi Filamentous ascomycetes harbor Woronin bodies and glyoxysomes two types of microbodies within one cell at the same time. The dominant protein of the Neurospora crassa Woronin body HEX1 forms a hexagonal core crystal via oligomerization and evidence has accumulated that Woro-nin bodies bud off from glyoxysomes. We analyzed whether HEX1 is sufficient to induce Woronin body formation upon heterologous expression in Saccharomyces cerevisiae an organism devoid of this specialized organelle. In wild-type strain BY4742 initial import of HEX1 into existing peroxisomes enabled the formation of organelles with a hexagonal crystal. The observed structures mimicked the shape of genuine Woronin bodies but exhibited a lower density and were significantly larger. Double-immunofluorescence analysis revealed that hexagonal HEX1 structures only occasionally co-localized with peroxisomal marker proteins indicating that the Woronin-body-like structures are well separated from peroxisomes. In cells lacking Vps1p and Dnm1p dynamin-like proteins required for the division of peroxisomes the Woronin-body-like organelles remained attached to peroxisomes. The data indicate that Woronin bodies emerge after the formation of a HEX1 core crystal within peroxisomes followed by Vps1p-and Dnm1p-mediated fission. The HEX1 .

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