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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

Visualisation of the Erp-Pδ Interaction Through the BiFC Assay.Strains carrying a) eyfpN + eyfpC, b) eyfpN + pδ-eyfpC, c) erp-eyfpN + eyfpC, and d) erp-eyfpN + pδ-eyfpC. Scale bars: 10 μm.
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f2: Visualisation of the Erp-Pδ Interaction Through the BiFC Assay.Strains carrying a) eyfpN + eyfpC, b) eyfpN + pδ-eyfpC, c) erp-eyfpN + eyfpC, and d) erp-eyfpN + pδ-eyfpC. Scale bars: 10 μm.

Mentions: Bimolecular fluorescence complementary analysis (BiFC) was performed to test the Erp-Pδ interaction in vivo. There were three negative controls (the strains expressing eyfpN + eyfpC, eyfpN + pδ-eyfpC, erp-eyfpN + eyfpC) in this experiment. None of them fluoresced (Fig. 2a–c). These results indicate the absence of autofluorescence or nonspecific background in the BiFC assay. However, the hyphae of the strains expressing erp-eyfpN and pδ-eyfpC exhibited yellow fluorescence (Fig. 2d). The yellow fluorescence in Fig. 2d suggests that Erp and Pδ are spatially close and interact with each other, forming a heterodimer in P. oxalicum.


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)

Visualisation of the Erp-Pδ Interaction Through the BiFC Assay.Strains carrying a) eyfpN + eyfpC, b) eyfpN + pδ-eyfpC, c) erp-eyfpN + eyfpC, and d) erp-eyfpN + pδ-eyfpC. Scale bars: 10 μm.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f2: Visualisation of the Erp-Pδ Interaction Through the BiFC Assay.Strains carrying a) eyfpN + eyfpC, b) eyfpN + pδ-eyfpC, c) erp-eyfpN + eyfpC, and d) erp-eyfpN + pδ-eyfpC. Scale bars: 10 μm.
Mentions: Bimolecular fluorescence complementary analysis (BiFC) was performed to test the Erp-Pδ interaction in vivo. There were three negative controls (the strains expressing eyfpN + eyfpC, eyfpN + pδ-eyfpC, erp-eyfpN + eyfpC) in this experiment. None of them fluoresced (Fig. 2a–c). These results indicate the absence of autofluorescence or nonspecific background in the BiFC assay. However, the hyphae of the strains expressing erp-eyfpN and pδ-eyfpC exhibited yellow fluorescence (Fig. 2d). The yellow fluorescence in Fig. 2d suggests that Erp and Pδ are spatially close and interact with each other, forming a heterodimer in P. oxalicum.

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