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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

Subcellular Distribution of Significantly Changed Proteins in Response to erp and pδ Deletions in P. oxalicum.
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f6: Subcellular Distribution of Significantly Changed Proteins in Response to erp and pδ Deletions in P. oxalicum.

Mentions: Intracellular proteomic analysis was performed using label-free liquid chromatography mass spectrometry to determine the intracellular response of P. oxalicum under cellulase-inducing conditions after p24 heterodimer disruption. Eighty-three proteins were significantly altered, and detailed information concerning these proteins is shown in Supplementary Information Table S1 online. According to published studies of homologues of these proteins3132, they were broadly distributed in the nuclear lumen, ER, Golgi-like apparatus, mitochondria, cytoskeleton, proteasome, and cytoplasm (Fig. 6).


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)

Subcellular Distribution of Significantly Changed Proteins in Response to erp and pδ Deletions in P. oxalicum.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f6: Subcellular Distribution of Significantly Changed Proteins in Response to erp and pδ Deletions in P. oxalicum.
Mentions: Intracellular proteomic analysis was performed using label-free liquid chromatography mass spectrometry to determine the intracellular response of P. oxalicum under cellulase-inducing conditions after p24 heterodimer disruption. Eighty-three proteins were significantly altered, and detailed information concerning these proteins is shown in Supplementary Information Table S1 online. According to published studies of homologues of these proteins3132, they were broadly distributed in the nuclear lumen, ER, Golgi-like apparatus, mitochondria, cytoskeleton, proteasome, and cytoplasm (Fig. 6).

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