Abstract
Komagataella phaffii yeast is one of the most important biocompounds producing microorganisms in modern biotechnology. Optimization of media recipes and cultivation strategies is key to successful synthesis of recombinant proteins. The complex effects of proline on gene expression in the yeast K. phaffii was analyzed on the transcriptome level in this work. Our analysis revealed drastic changes in gene expression when K. phaffii was grown in proline-containing media in comparison to ammonium sulphate-containing media. Around 18.9% of all protein-encoding genes were differentially expressed in the experimental conditions. Proline is catabolized by K. phaffii even in the presence of other nitrogen, carbon and energy sources. This results in the repression of genes involved in the utilization of other element sources, namely methanol. We also found that the repression of AOX1 gene promoter with proline can be partially reversed by the deletion of the KpPUT4.2 gene.
Highlights
Expression in the YeastOne of the main aspects of modern biotechnology is the synthesis of peptides and recombinant proteins of various origins and for various applications
We studied the expression of KpPUT1 gene (PAS_chr1-3_0269) in K. phaffii yeast, which is the ortholog of the S. cerevisiae PUT1 gene
K. phaffii P1AP-GS115 strain has been constructed in our lab
Summary
One of the main aspects of modern biotechnology is the synthesis of peptides and recombinant proteins of various origins and for various applications. Komagataella phaffii ( known as Pichia pastoris) yeast is one of the most promising biotechnologically-relevant microorganisms, actively used as a microbial cell factory for large-scale recombinant protein production [1,2]. The successful use of K. phaffii in biotechnology, the pharmaceutical industry, and the food industry is largely due to the favorable characteristics of its metabolism. This yeast is methylotrophic, i.e., it is capable of using methanol as the sole carbon and energy source in the growth medium, thanks to a whole set of enzymes and their corresponding genes.
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