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If the constructive evolution of mitochondrial ribosomes and OXPHOS complexes was indeed driven by (slightly) deleterious mutation accumulation in mitochondrial genes, then it should be possible to detect mutational effects in the sequences and/or products of those genes in contemporary eukaryotes.
(C) Mutational effects in the amphipathic helix α6-7.
(D) Mutational effects in the region of titratable key residues.
(B) Mutational effects in the two signaling motif regions.
The similarity of these mutational effects in regard to craniofacial geometry suggests a common developmental mechanism.
Although we observe a correlation between the severity of the mutational effects in vitro and in vivo, we also detect a number of notable exceptions to this rule.
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Previous investigations have demonstrated that the 249ser TP53 mutation is a biomarker of the aflatoxin-associated mutational effect in the p53 gene (Aguilar et al. 1993; Mace et al. 1997); methods for detection of the 249ser TP53 mutation in plasma have been previously described (Kirk et al. 2000, 2005; Szymanska et al. 2004).
Moreover, chaperones have been shown to buffer mutational effects both in eukaryotes and in prokaryotes (Rutherford 2003).
Figure 5 shows how the mutational effects changed in the five different backgrounds in a comprehensive manner.
Figure 7 compares the mutational effects determined in our study to those from Wu et al. (2014).
DOI: http://dx.doi.org/10.7554/eLife.00631.030 This caveat about R384G and E375G notwithstanding, it is striking that we can explain all of the other observed mutational effects simply in terms of protein stability.
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