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Function of a p24 Heterodimer in Morphogenesis and Protein Transport in Penicillium oxalicum.

Wang F, Liu K, Han L, Jiang B, Wang M, Fang X - Sci Rep (2015)

Bottom Line: The results suggested that the p24 heterodimer mediates protein transport, particularly that of cellobiohydrolase.These results suggest that the p24 heterodimer participates in morphogenesis and protein transport.Compared with P. oxalicum Δerp, a greater number of cellular physiological pathways were impaired in ΔerpΔpδ.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, China.

ABSTRACT
The lignocellulose degradation capacity of filamentous fungi has been widely studied because of their cellulase hypersecretion. The p24 proteins in eukaryotes serve important functions in this secretory pathway. However, little is known about the functions of the p24 proteins in filamentous fungi. In this study, four p24 proteins were identified in Penicillium oxalicum. Six p24 double-deletion strains were constructed, and further studies were carried out with the ΔerpΔpδ strain. The experimental results suggested that Erp and Pδ form a p24 heterodimer in vivo. This p24 heterodimer participates in important morphogenetic events, including sporulation, hyphal growth, and lateral branching. The results suggested that the p24 heterodimer mediates protein transport, particularly that of cellobiohydrolase. Analysis of the intracellular proteome revealed that the ΔerpΔpδ double mutant is under secretion stress due to attempts to remove proteins that are jammed in the endomembrane system. These results suggest that the p24 heterodimer participates in morphogenesis and protein transport. Compared with P. oxalicum Δerp, a greater number of cellular physiological pathways were impaired in ΔerpΔpδ. This finding may provide new insights into the secretory pathways of filamentous fungi.

No MeSH data available.


Related in: MedlinePlus

Comparison of the Sporulation Efficiencies of the Parent and ΔerpΔpδ Strains.*P < 0.05, **P < 0.01. Panel a, phenotypic analysis of the parent and ΔerpΔpδ strains on wheat bran plates. Panel b, the number of spores produced per square centimetre on wheat bran plates. Panel c, the number of spores produced per milligram of mycelial protein in submerged cultivation. Error bars indicate the standard deviation calculated from three biological experiments.
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f3: Comparison of the Sporulation Efficiencies of the Parent and ΔerpΔpδ Strains.*P < 0.05, **P < 0.01. Panel a, phenotypic analysis of the parent and ΔerpΔpδ strains on wheat bran plates. Panel b, the number of spores produced per square centimetre on wheat bran plates. Panel c, the number of spores produced per milligram of mycelial protein in submerged cultivation. Error bars indicate the standard deviation calculated from three biological experiments.

Mentions: The roles of Erp in T. reesei and P. oxalicum were investigated. Sporulation on wheat bran plates was drastically reduced for T. reesei Δerp but not P. oxalicum Δerp (spore production was quantified by counting the number of spores per square centimetre using a haemocytometer)27. Therefore, approximately 1 × 107 spores were inoculated onto wheat bran plates at 30 °C for 3 d to detect whether the sporulation pathway was impaired in the ΔerpΔpδ strain (see Supplementary Information Fig. S3 online for Southern blotting analysis of pδ). The number of spores was significantly reduced in the ΔerpΔpδ strain (P = 0.0054, n = 18) (Fig. 3b). To further confirm this result, comparison of the sporulation levels of the parent and ΔerpΔpδ strains during submerged cultivation was performed. The number of spores was significantly decreased for the ΔerpΔpδ strain (P = 0.017, n = 5) (Fig. 3c). Therefore, this finding suggests that the ΔerpΔpδ strain is likely to be defective in sporulation.


Function of a p24 Heterodimer in Morphogenesis and Protein Transport in Penicillium oxalicum.

Wang F, Liu K, Han L, Jiang B, Wang M, Fang X - Sci Rep (2015)

Comparison of the Sporulation Efficiencies of the Parent and ΔerpΔpδ Strains.*P < 0.05, **P < 0.01. Panel a, phenotypic analysis of the parent and ΔerpΔpδ strains on wheat bran plates. Panel b, the number of spores produced per square centimetre on wheat bran plates. Panel c, the number of spores produced per milligram of mycelial protein in submerged cultivation. Error bars indicate the standard deviation calculated from three biological experiments.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493713&req=5

f3: Comparison of the Sporulation Efficiencies of the Parent and ΔerpΔpδ Strains.*P < 0.05, **P < 0.01. Panel a, phenotypic analysis of the parent and ΔerpΔpδ strains on wheat bran plates. Panel b, the number of spores produced per square centimetre on wheat bran plates. Panel c, the number of spores produced per milligram of mycelial protein in submerged cultivation. Error bars indicate the standard deviation calculated from three biological experiments.
Mentions: The roles of Erp in T. reesei and P. oxalicum were investigated. Sporulation on wheat bran plates was drastically reduced for T. reesei Δerp but not P. oxalicum Δerp (spore production was quantified by counting the number of spores per square centimetre using a haemocytometer)27. Therefore, approximately 1 × 107 spores were inoculated onto wheat bran plates at 30 °C for 3 d to detect whether the sporulation pathway was impaired in the ΔerpΔpδ strain (see Supplementary Information Fig. S3 online for Southern blotting analysis of pδ). The number of spores was significantly reduced in the ΔerpΔpδ strain (P = 0.0054, n = 18) (Fig. 3b). To further confirm this result, comparison of the sporulation levels of the parent and ΔerpΔpδ strains during submerged cultivation was performed. The number of spores was significantly decreased for the ΔerpΔpδ strain (P = 0.017, n = 5) (Fig. 3c). Therefore, this finding suggests that the ΔerpΔpδ strain is likely to be defective in sporulation.

Bottom Line: The results suggested that the p24 heterodimer mediates protein transport, particularly that of cellobiohydrolase.These results suggest that the p24 heterodimer participates in morphogenesis and protein transport.Compared with P. oxalicum Δerp, a greater number of cellular physiological pathways were impaired in ΔerpΔpδ.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, China.

ABSTRACT
The lignocellulose degradation capacity of filamentous fungi has been widely studied because of their cellulase hypersecretion. The p24 proteins in eukaryotes serve important functions in this secretory pathway. However, little is known about the functions of the p24 proteins in filamentous fungi. In this study, four p24 proteins were identified in Penicillium oxalicum. Six p24 double-deletion strains were constructed, and further studies were carried out with the ΔerpΔpδ strain. The experimental results suggested that Erp and Pδ form a p24 heterodimer in vivo. This p24 heterodimer participates in important morphogenetic events, including sporulation, hyphal growth, and lateral branching. The results suggested that the p24 heterodimer mediates protein transport, particularly that of cellobiohydrolase. Analysis of the intracellular proteome revealed that the ΔerpΔpδ double mutant is under secretion stress due to attempts to remove proteins that are jammed in the endomembrane system. These results suggest that the p24 heterodimer participates in morphogenesis and protein transport. Compared with P. oxalicum Δerp, a greater number of cellular physiological pathways were impaired in ΔerpΔpδ. This finding may provide new insights into the secretory pathways of filamentous fungi.

No MeSH data available.


Related in: MedlinePlus