Enhancing the Secretion Efficiency of Heterologous Proteins in Pichia pastoris through N-Glycosylation and SOD1-Mediated Redox Regulation
This project presents the RNA seq data generated from two engineered strains of the methylotrophic yeast Pichia pastoris GS115, which exhibit differential secretion efficiencies for enhanced green fluorescent protein. These strains, designated GS115-High and GS115-Low, were constructed through site-directed mutagenesis of glycosylation sites within the alpha-mating factor signal peptide. The primary objective of this study was to investigate the global transcriptional mechanisms underlying divergent protein secretion capacities. Comparative transcriptomic analysis between the high and low secretion strains revealed significant upregulation of the superoxide dismutase gene and enhanced oxidoreductase activity in the GS115-High strain, suggesting a critical link between efficient protein secretion and robust cellular antioxidant defense. Additionally, pathways related to amino acid metabolism were notably altered, indicating a synergistic reallocation of metabolic resources. This dataset provides valuable insights into the cooperative interplay between protein processing and redox homeostasis, serving as a key resource for understanding and engineering P. pastoris for improved heterologous protein production.