The polarisome component SpaA localises to hyphal tips of Aspergillus niger and is important for polar growth.
Hyphal tip growth is a key feature of filamentous fungi, however, the molecular mechanism(s) that regulate cell polarity are poorly understood. On the other hand, much more is known about polarised growth in the yeast Saccharomyces cerevisiae. Here, the proteins Spa2p, Bni1p, Bud6p and Pea2p form a protein complex named the polarisome known to be important for the assurance of polar growth. We searched the genome of Aspergillus niger and identified homologues for Spa2p, Bni1p, Bud6p but not for Pea2p. We characterised the function of the Spa2p homologue SpaA by determining its cellular localisation and by constructing deletion and overexpressing mutant strains. SpaA was found to be localised exclusively at the hyphal tip, suggesting that SpaA can be used as marker for polarisation. Deletion and overexpression of spaA resulted in reduced growth rate, increased hyphal diameter and polarity defects, indicating that one of the functions of SpaA is to ensure polarity maintenance. In addition, we could show that SpaA is able to complement the defective haploid invasive growth phenotype of a S. cerevisiae SPA2 null mutant. We suggest that the function of SpaA is to ensure maximal polar growth rate in A. niger.
Meyer
Vera
V
Department of Microbiology and Genetics, Institute of Biotechnology, Berlin University of Technology, Gustav-Meyer-Allee 25, D-13355 Berlin, Germany. v.meyer@lb.tu-berlin.de
Arentshorst
Mark
M
van den Hondel
Cees A M J J
CA
Ram
Arthur F J
AF
D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000502:physiology*; D016764:Cell Polarity; D005656:Fungal Proteins / Q000502:physiology*; D005800:Genes, Fungal; D025301:Hyphae / Q000254:growth & development* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment