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Changes in mitochondrial function may impact protein metabolism since protein synthesis and ubiquitin-dependent protein degradation are ATP-dependent.

The observation that numerous TS lethal, and not other TS mutants, are involved in protein synthesis, transport, or, as suggested by the current study, protein quality control (Table 4), implies that additional TS lethal mutants generated by Inoue and colleagues in Neurospora [4] may impact protein synthesis pathways.

Therefore, such local conformational changes may impact protein function and may cause disease.

Altogether these observations indicate that the acquisition of drug-resistance mutations in pfcrt may impact protein synthesis and turnover pathways.

Evidence for positive selection was found for one of these, the CSRP3 gene, which also had a substitution that may impact protein function (Zhao et al. 2010).

As RO4929097 is highly bound in plasma to α1-acid glycoprotein and albumin, monitoring of unbound RO4929097 has been recommended particularly when it is administered with other compounds that may impact protein binding (Wu et al, 2012).

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Even though out-of-frame sequence between compensatory indels is short (<6 bp) in our B. chromaiodes – B. pennsylvanicus comparison, these indels result in one or two amino acid substitutions (fig. 1), suggesting that compensatory indels may also impact protein divergence in endosymbiont genomes.

In this case, SIFT analysis indicate that the two mutations may impact the protein function.

This location represents a different biochemical environment than intracellular spaces and therefore may impact foreign protein stability.

The mechanisms by which genotype may impact GRα protein isoform levels in a brain region-specific manner remain to be elucidated.

We then identify substitutions at these sites within the three Nasonia species that violate this constraint and therefore may impact the protein structure and ultimately the function of the gene.

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