Septal pore cap protein SPC18, isolated from the basidiomycetous fungus Rhizoctonia solani, also resides in pore plugs
| Autor: | Arie J. Verkleij, Arend F. van Peer, Wally H. Müller, Han A. B. Wösten, Kenneth G.A. van Driel, Teun Boekhout, Jan Grijpstra |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Hypha
Molecular Sequence Data Hyphae Microbiology Rhizoctonia Fungal Proteins Agaricomycotina Organelle Life Science Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Glycoproteins Fungal protein biology Base Sequence Endoplasmic reticulum fungi Basidiomycota General Medicine Articles biology.organism_classification Cell biology Protein Transport Ultrastructure |
| Zdroj: | Eukaryotic Cell, 7(10), 1865-1873 Eukaryotic Cell 7 (2008) 10 Eukaryotic Cell, 7(10), 1865-1873. American Society for Microbiology |
| ISSN: | 1535-9778 |
| Popis: | The hyphae of filamentous fungi are compartmentalized by septa that have a central pore. The fungal septa and septum-associated structures play an important role in maintaining cellular and intrahyphal homeostasis. The dolipore septa in the higher Basidiomycota (i.e., Agaricomycotina ) are associated with septal pore caps. Although the ultrastructure of the septal pore caps has been studied extensively, neither the biochemical composition nor the function of these organelles is known. Here, we report the identification of the glycoprotein SPC18 that was found in the septal pore cap-enriched fraction of the basidiomycetous fungus Rhizoctonia solani . Based on its N-terminal sequence, the SPC18 gene was isolated. SPC18 encodes a protein of 158 amino acid residues, which contains a hydrophobic signal peptide for targeting to the endoplasmic reticulum and has an N-glycosylation motif. Immunolocalization showed that SPC18 is present in the septal pore caps. Surprisingly, we also observed SPC18 being localized in some plugs. The data reported here strongly support the hypothesis that septal pore caps are derived from endoplasmic reticulum and are involved in dolipore plugging and, thus, contribute to hyphal homeostasis in basidiomycetous fungi. |
| Databáze: | OpenAIRE |
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