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Updated: Aug 8, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Association of 70-kilodalton heat-shock cognate proteins with acclimation to cold
L G Neven1, D W Haskell, C L Guy
1Department of Environmental Horticulture, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, Florida 32611.
Abstract:
Exposure of young spinach seedlings (Spinacia oleracea L. cv Bloomsdale) to 5 degrees C leads to an increase in the synthesis of several 79-kilodalton proteins that are present in leaf tissue grown at 20 degrees C. Protein sequence analyses and immunological cross-reactivity indicate that this group of proteins belongs to the 70-kilodalton heat-shock family. Steady-state transcript levels and protein synthesis are increased two- to threefold within 1 day, but immunoblot analyses suggest that the steady-state concentration of this protein group in leaf tissue only gradually accumulates at low temperature. It is proposed that the increased synthesis of several members of the 70-kilodalton heat-shock family could result from an influence of low temperature on protein folding and/or assembly processes.
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