Mutations in proteins of the Conserved Oligomeric Golgi Complex affect polarity, cell wall structure, and glycosylation in the filamentous fungus Aspergillus nidulans

S. K. Gremillion, S. D. Harris, L. Jackson-Hayes, S. G.W. Kaminskyj, D. M. Loprete, A. C. Gauthier, S. Mercer, A. J. Ravita, T. W. Hill

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

We have described two Aspergillus nidulans gene mutations, designated podB1 (polarity defective) and swoP1 (swollen cell), which cause temperature-sensitive defects during polarization. Mutant strains also displayed unevenness and abnormal thickness of cell walls. Un-polarized or poorly-polarized mutant cells were capable of establishing normal polarity after a shift to a permissive temperature, and mutant hyphae shifted from permissive to restrictive temperature show wall and polarity abnormalities in subsequent growth. The mutated genes ( podB= AN8226.3; swoP= AN7462.3) were identified as homologues of COG2 and COG4, respectively, each predicted to encode a subunit of the multi-protein COG (Conserved Oligomeric Golgi) Complex involved in retrograde vesicle trafficking in the Golgi apparatus. Down-regulation of COG2 or COG4 resulted in abnormal polarization and cell wall staining. The GFP-tagged COG2 and COG4 homologues displayed punctate, Golgi-like localization. Lectin-blotting indicated that protein glycosylation was altered in the mutant strains compared to the wild type. A multicopy expression experiment showed evidence for functional interactions between the homologues COG2 and COG4 as well as between COG2 and COG3. To date, this work is the first regarding a functional role of the COG proteins in the development of a filamentous fungus.

Original languageEnglish (US)
Pages (from-to)69-82
Number of pages14
JournalFungal Genetics and Biology
Volume73
DOIs
StatePublished - Dec 1 2014

Fingerprint

Aspergillus nidulans
Golgi Apparatus
Glycosylation
Cell Wall
Fungi
Mutation
Temperature
Proteins
Hyphae
Protein Subunits
Lectins
Genes
Down-Regulation
Staining and Labeling
Growth

Keywords

  • Aspergillus nidulans
  • COG complex
  • Cell wall
  • Glycosylation
  • Polarity maintenance

ASJC Scopus subject areas

  • Microbiology
  • Genetics

Cite this

Mutations in proteins of the Conserved Oligomeric Golgi Complex affect polarity, cell wall structure, and glycosylation in the filamentous fungus Aspergillus nidulans. / Gremillion, S. K.; Harris, S. D.; Jackson-Hayes, L.; Kaminskyj, S. G.W.; Loprete, D. M.; Gauthier, A. C.; Mercer, S.; Ravita, A. J.; Hill, T. W.

In: Fungal Genetics and Biology, Vol. 73, 01.12.2014, p. 69-82.

Research output: Contribution to journalArticle

Gremillion, S. K. ; Harris, S. D. ; Jackson-Hayes, L. ; Kaminskyj, S. G.W. ; Loprete, D. M. ; Gauthier, A. C. ; Mercer, S. ; Ravita, A. J. ; Hill, T. W. / Mutations in proteins of the Conserved Oligomeric Golgi Complex affect polarity, cell wall structure, and glycosylation in the filamentous fungus Aspergillus nidulans. In: Fungal Genetics and Biology. 2014 ; Vol. 73. pp. 69-82.
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AU - Gremillion, S. K.

AU - Harris, S. D.

AU - Jackson-Hayes, L.

AU - Kaminskyj, S. G.W.

AU - Loprete, D. M.

AU - Gauthier, A. C.

AU - Mercer, S.

AU - Ravita, A. J.

AU - Hill, T. W.

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AB - We have described two Aspergillus nidulans gene mutations, designated podB1 (polarity defective) and swoP1 (swollen cell), which cause temperature-sensitive defects during polarization. Mutant strains also displayed unevenness and abnormal thickness of cell walls. Un-polarized or poorly-polarized mutant cells were capable of establishing normal polarity after a shift to a permissive temperature, and mutant hyphae shifted from permissive to restrictive temperature show wall and polarity abnormalities in subsequent growth. The mutated genes ( podB= AN8226.3; swoP= AN7462.3) were identified as homologues of COG2 and COG4, respectively, each predicted to encode a subunit of the multi-protein COG (Conserved Oligomeric Golgi) Complex involved in retrograde vesicle trafficking in the Golgi apparatus. Down-regulation of COG2 or COG4 resulted in abnormal polarization and cell wall staining. The GFP-tagged COG2 and COG4 homologues displayed punctate, Golgi-like localization. Lectin-blotting indicated that protein glycosylation was altered in the mutant strains compared to the wild type. A multicopy expression experiment showed evidence for functional interactions between the homologues COG2 and COG4 as well as between COG2 and COG3. To date, this work is the first regarding a functional role of the COG proteins in the development of a filamentous fungus.

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