N-Glycosylation is a common form of protein post-translational modification in Pichia pastoris and greatly affects folding and secretion. The propeptide of the Pseudomonas aeruginosa elastase (PAE) is indispensable for proper folding and secretion of the enzyme. We have studied the effect of introducing N-glycosylation sites to the propeptide of the recombinant elastase (rPAE) on its expression levels in P. pastoris. Addition of N-glycosylation sites to the propeptide at N51 or N93 enhanced rPAE production levels by 104 or 57%, respectively, while addition at N11 or N127 led to a 25 or 50% decrease, respectively. The introduced N-glycosylation sites in the propeptide at these four sites exerted a null effect on the N-glycosylation degree of mature rPAE.
The mitochondrial genome of the Platencyrtus parkeri Feriere (Hymenoptera: Encyrtidae) was obtained via next-generation sequencing. The assembled mitogenome is 13,393 bp in length, which contains 33 classical eukaryotic mitochondrial genes with three tRNA genes and rrnS gene missing. All the 13 PCGs begin with typical ATN codons. The 19 detected tRNAs range from 58 to 70 bp in length with typical cloverleaf structure except for trnS1, whose dihydrouridine (DHU) arm forms a simple loop. Meanwhile, they have six tRNAs inserted between nad2 and nad3 compared with Encyrtus infelix. Phylogenetic analysis highly supported the monophyly of Pteromalidae. Eupelmidae and Encyrtidae have a close relationship. Within Encyrtidae, Platencyrtus parkeri Feriere and Encyrtus infelix are close to each other.
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