Between genotype and phenotype: protein chaperones and evolvability View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-04

AUTHORS

Suzanne L Rutherford

ABSTRACT

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. More... »

PAGES

263-274

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nrg1041

    DOI

    http://dx.doi.org/10.1038/nrg1041

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1018646325

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12671657


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