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In the laboratory, the Drosophila melanogaster heat shock protein Hsp90 can buffer the phenotypic effects of genetic variation.
As outlined in the introduction, the idea that molecular chaperones buffer the phenotypic effects of mutations in their clients is critical to the hypothesis that chaperones facilitate adaptive evolution (Rutherford and Lindquist 1998; Tokuriki and Tawfik 2009a).
One of the best-studied aspects of Hsp90 function in laboratory populations is the ability of Hsp90 to buffer the phenotypic effects of genetic variation [ 7, 8, 16, 22].
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Genes required to buffer the phenotypic consequences of mutations in other loci were identified using synthetic lethal genetic interaction screens.
The pioneering work in this area was that of Rutherford and Lindquist (1998), who demonstrated that the chaperone Hsp90 suppresses (or buffers) the phenotypic effect of deleterious mutations in its clients, which are mainly signaling proteins.
The phenotypic effects of deleterious mutations can be buffered by overproduction of molecular chaperones, of which GroEL and DnaK are the two most important and best studied [ 32, 34].
Only then can biological functions of the true targets be connected to the phenotypic effects of the ligand.
Indeed inhibiting the activity of DYRK1A may counteract the phenotypic effects of its overexpression.
The phenotypic effects of r84 therapy within NSCLC tumors were assessed by immunohistochemistry (IHC).
To dissect the phenotypic effects of ssadh mutations, we first crossed ssadh mutants with pop2 mutants.
Finally, the phenotypic effects of most mutations are restricted to specific pathways and/or processes.
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