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. 2020 Sep 29;10:15983. doi: 10.1038/s41598-020-72410-y

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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(A) GO analysis of stable and unstable protein datasets demonstrated significant enrichment of different subcellular components. The four most significantly enriched localizations are reported. Y-axis represents the negative log₂ of p-value of enrichment. B) The percentage of mitochondrial proteins quantified in each tissue dataset is shown in Fig. 2F. (C) Re-analysis of the data in Fig. 2F. Comparison of the average Day7/Day0 protein ratio of mitochondrial (“mito” in red) and non-mitochondrial (“non-mito” in black) proteins in different tissues. One-way ANOVA analysis test computed a p-value of < 0.0001. All p-values from a post-hoc Tukey’s multiple comparisons test are in Table S9. The significant differences to the brain non-mitochondrial dataset from the Tukey’s test are shown in the figure. (D) Immunoblot analysis confirmed differences in stability between a translational (EIF2α) and a cytoskeletal (β-actin) protein. Click reaction was performed on brain homogenates from three mice at 3 day and 14 day. Samples were analyzed before (Input) and after (AHA) neutravidin enrichment. The images represent four separately processed immunoblots. The uncropped immunoblot images are in Fig. S8. (E) Significant difference between the stability of actin and EIF2α was observed with immunoblot analysis. Quantification of the pixel intensity of the immunoreactivity of the enrichment samples in Fig. 3D demonstrated a larger significant (p < 0.05*) difference between 3 and 14 day with EIF2α than with actin. The y-axis shows the percent decrease in immunoreactivity between 3 and 14 day. A two-tailed t-test was performed. (F) Significant differences in the stability of different TRIC complex subunits were observed in brain tissue. The average protein heavy/light ratio from biological replicates at each time point was plotted for subunits of the TRiC complex from brain tissue. One-way ANOVA analysis was performed on the subunit ratios at each time point. There was a significant difference observed at 7 day(p < 0.01 ) and 14 day(p < 0.0001). Multiple Comparison post-hoc test was performed to determine which subunits were significantly different. At 7 day, CCT4 vs CCT6a* and CCT4 vs CCT8*. At 14 day, CCT4 vs CCT6a***,CCT4 vs CCT7*, and CCT4 vs CCT8**, CCT5 vs CCT6a****, CCT5 vs CCT7**, and CCT5 vs CCT8***. Figures depict the Bonferroni's p-values. *p < 0.05, **p < 0.01, ***p < 0.001,****p < 0.0001.