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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 Protein Secretion Capabilities of the Parent and ΔerpΔpδ Strains.Panel a, comparison of extracellular protein concentrations and enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Panel b, comparison of intracellular protein concentrations and specific enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Error bars indicate the standard deviation calculated from three biological experiments.
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f5: Comparison of the Protein Secretion Capabilities of the Parent and ΔerpΔpδ Strains.Panel a, comparison of extracellular protein concentrations and enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Panel b, comparison of intracellular protein concentrations and specific enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Error bars indicate the standard deviation calculated from three biological experiments.

Mentions: Equal quantities of precultured mycelia were inoculated into liquid media containing 2% Avicel to compare the relative protein secretion capabilities of the parent and ΔerpΔpδ strains. CMCase, pNPCase and xylanase activities represent endoglucanase, cellobiohydrolase and xylanase activities, respectively. The results for the extracellular enzymatic activities normalised to intracellular proteins are shown in Fig. 5a. For the ΔerpΔpδ strain, extracellular pNPCase activity significantly decreased after 48 hours of cultivation (P < 0.05, n = 3). The extracellular protein concentration significantly decreased in the ΔerpΔpδ strain after 72 hours following inoculation (P < 0.05, n = 3). However, CMCase and xylanase activities were not significantly changed in the ΔerpΔpδ strain. Intracellular specific enzymatic activities were also detected. As shown in Fig. 5b, there were no significant differences between specific CMCase and xylanase activities. However, specific pNPCase activity significantly increased at 24, 48, and 96 hours after inoculation (P < 0.05, n = 3). Therefore, protein secretion declined in the ΔerpΔpδ strain. This suggests that the p24 heterodimer is likely involved in protein transport, particularly in the transport of cellobiohydrolase.


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 Protein Secretion Capabilities of the Parent and ΔerpΔpδ Strains.Panel a, comparison of extracellular protein concentrations and enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Panel b, comparison of intracellular protein concentrations and specific enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. 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

f5: Comparison of the Protein Secretion Capabilities of the Parent and ΔerpΔpδ Strains.Panel a, comparison of extracellular protein concentrations and enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Panel b, comparison of intracellular protein concentrations and specific enzymatic activities between the parent and ΔerpΔpδ strains. Closed square, parent strain; open square, ΔerpΔpδ strain. Error bars indicate the standard deviation calculated from three biological experiments.
Mentions: Equal quantities of precultured mycelia were inoculated into liquid media containing 2% Avicel to compare the relative protein secretion capabilities of the parent and ΔerpΔpδ strains. CMCase, pNPCase and xylanase activities represent endoglucanase, cellobiohydrolase and xylanase activities, respectively. The results for the extracellular enzymatic activities normalised to intracellular proteins are shown in Fig. 5a. For the ΔerpΔpδ strain, extracellular pNPCase activity significantly decreased after 48 hours of cultivation (P < 0.05, n = 3). The extracellular protein concentration significantly decreased in the ΔerpΔpδ strain after 72 hours following inoculation (P < 0.05, n = 3). However, CMCase and xylanase activities were not significantly changed in the ΔerpΔpδ strain. Intracellular specific enzymatic activities were also detected. As shown in Fig. 5b, there were no significant differences between specific CMCase and xylanase activities. However, specific pNPCase activity significantly increased at 24, 48, and 96 hours after inoculation (P < 0.05, n = 3). Therefore, protein secretion declined in the ΔerpΔpδ strain. This suggests that the p24 heterodimer is likely involved in protein transport, particularly in the transport of cellobiohydrolase.

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