Bacteria respond to an abrupt decrease in temperature with a specific
response, in which cold-induced proteins (CIPs) are transiently expres
sed at a higher level. Employing two-dimensional gel electrophoresis,
several CIPs have been identified. In spite of this, the overall funct
ion of the cold shock response is unclear. Recently, the main attentio
n has focused on a group of conserved cold shock proteins (CSPs) that
have been shown to have the highest induction after cold shock and to
play a major regulatory role in the physiology of adaptation to low te
mperatures. CSPs, of which Escherichia coli, Bacillus subtilis, and B.
cereus possess a family comprising at least 3-7 proteins, are small a
cidic proteins that share over 45% of sequence identity. Recent eviden
ce suggests that members of this wide-spread protein family can functi
on both at the transcriptional and translational level in vitro. Howev
er, the exact mode of action has yet to be established. In addition, p
ost-transcriptional regulation seems to play a major role in the induc
tion of CSPs, a process in which the ribosome may be involved. This is
in accordance with a model in which the ribosome has been proposed to
be the sensor of temperature in bacteria.