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The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion

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Abstract

Glycosylphosphatidylinositol (GPI) anchoring is the main mechanism allowing proper localization of secretory proteins in cell membranes. We have isolated an Aspergillus nidulans homolog of the human PIG-P gene, which encodes a subunit of acetylglucosaminyltransferase (GPI-GnT)—an enzyme involved in the synthesis of GPI anchors. A. nidulans pigP mutants have significantly decreased GPI synthesis. On solid media they show strong growth retardation (the “button” phenotype) while in liquid minimal media they show overall good growth but with hyperbranched and bulbous hyphae with impaired septation. Furthermore, the pigP strains, in contrast to the wild-type, abundantly secrete a 33-kDa alkaline serine protease (ALP) into the liquid medium.

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Acknowledgments

We are indebted to M. Hoffman-Sommer and H. Sierakowska for critical reading and correction of the manuscript. This work was supported by the State Committee for Scientific Research, grant number 2P04A04628 to A. P.

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Correspondence to Sebastian Piłsyk.

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Communicated by G. Braus.

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Piłsyk, S., Paszewski, A. The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion. Curr Genet 55, 301–309 (2009). https://doi.org/10.1007/s00294-009-0246-x

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  • DOI: https://doi.org/10.1007/s00294-009-0246-x

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