The role of cold-shock proteins in low-temperature adaptation of food-related bacteria.
There is a considerable interest in the cold adaptation of food-related bacteria, including starter cultures for industrial food fermentations, food spoilage bacteria and food-borne pathogens. Mechanisms that permit low-temperature growth involve cellular modifications for maintaining membrane fluidity, the uptake or synthesis of compatible solutes, the maintenance of the structural integrity of macromolecules and macromolecule assemblies, such as ribosomes and other components that affect gene expression. A specific cold response that is shared by nearly all food-related bacteria is the induction of the synthesis so-called cold-shock proteins (CSPs), which are small (7 kDa) proteins that are involved in mRNA folding, protein synthesis and/or freeze protection. In addition, CSPs are able to bind RNA and it is believed that these proteins act as RNA chaperones, thereby reducing the increased secondary folding of RNA at low temperatures. In this review established and novel aspects concerning the structure, function and control of these CSPs are discussed. A model for bacterial cold adaptation, with a central role for ribosomal functioning, and possible mechanisms for low-temperature sensing are discussed.
Laboratory of Food Microbiology, Wageningen University, Wageningen Centre for Food Sciences, The Netherlands.
J A
JA
Wouters
F M
FM
Rombouts
O P
OP
Kuipers
W M
WM
de Vos
T
T
Abee
D000220:Adaptation, Biological / Q000235:genetics*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D003080:Cold Temperature; D005516:Food Microbiology; D008957:Models, Genetic; D018832:Molecular Chaperones / Q000378:metabolism; D008969:Molecular Sequence Data; D016601:RNA-Binding Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D018832:Molecular Chaperones; D016601:RNA-Binding Proteins