Between genotype and phenotype: protein chaperones and evolvability.
Protein chaperones direct the folding of polypeptides into functional proteins, facilitate developmental signalling and, as heat-shock proteins (HSPs), can be indispensable for survival in unpredictable environments. Recent work shows that the main HSP chaperone families also buffer phenotypic variation. Chaperones can do this either directly through masking the phenotypic effects of mutant polypeptides by allowing their correct folding, or indirectly through buffering the expression of morphogenic variation in threshold traits by regulating signal transduction. Environmentally sensitive chaperone functions in protein folding and signal transduction have different potential consequences for the evolution of populations and lineages under selection in changing environments.
Rutherford
Suzanne L
SL
Division of Basic Sciences, Fred Hutchinson Cancer Research Centre, Mailstop A2-168, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA. srutherf@fhcrc.org
D000818:Animals; D019143:Evolution, Molecular; D005838:Genotype; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D015394:Molecular Structure; D009154:Mutation; D010641:Phenotype; D017510:Protein Folding; D015398:Signal Transduction
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones