Fig. 4

Co-translational folding efficiency of Phy nascent chains and protein aggregates in RP deletion strains. a Assessment of co-translational folding efficiency of Phy nascent chains in wild-type and RP deletion strains. After the limited proteinase K digestion, samples were separated by SDS-PAGE, and the remaining Phy was visualized by western blotting. The optical density of Phy band was calculated and the RNC aliquots from the same samples with proteinase K digestion were normalized to those with no proteinase K digestion. b Quantitative analysis of protein aggregates extracted from wild-type and RP deletion strains transformed with Phy which is glycosylated in P. pastoris [57]. The samples were subject to SDS-PAGE separation followed by Coomassie blue staining, and Phy was visualized by western blotting. c Quantification of Phy aggregate level as shown in b. The aggregated Phy signals were normalized to totals and wild-type strain transformed with Phy was set as 100%. Unpaired t test of GraphPad Prism 6 was used for statistical analysis. Significant difference of Phy aggregates level is indicated as: *p < 0.05; **p < 0.01; ***p < 0.001. Error bars represent s.d. of at least three independent experiments