Bacterial Adaptation to Low Temperature: Implications for Cold-Inducible Genes |
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Authors: | Noriyuki Fukunaga Takehiko Sahara Yasuhiro Takada |
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Institution: | (1) Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, 060–0810 Japan, JP |
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Abstract: | Escherichia coli and later found to be a cold-shock response common to many bacterial species. CspA of 7.4 kD, a major cold-shock protein
in E. coli, has been shown to share structural similarity with a class of eukaryotic Y box proteins which have RNA-binding domains.
Transient synthesis of CspA upon cold shock is mediated by increased stabilization of the mRNA at low temperatures. The proposed
role of some cold-shock proteins including CspA in the bacterial adaptation to low temperatures is to function as a RNA chaperone
in the regulation of translation. Some enzymes of psychrotrophic or psychrophilic bacteria exhibit unique features of a cold-adapted
enzyme, high catalytic activity at a low temperature and rapid inactivation at a moderate temperature. A monomeric isocitrate
dehydrogenase isozyme (IDH-II) of a psychrophilic bacterium, Vibrio sp. strain ABE-1, is a typical cold-adapted enzyme. In addition, this enzyme is induced at low temperatures. Low temperature-dependent
expression of icdll encoding IDH-II is controlled by two different cis-elements located at the untranslated upstream region of the gene, one is a silencer and the other is essential for the low
temperature response. The physiological role of IDH-II is evaluated by transforming E. coli with icdll. The growth rate of the E. coli transformants at low temperatures is dependent on the level of expressed IDH-II activity.
Received 11 January 1999/ Accepted in revised form 6 April 1999 |
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Keywords: | : Cold-adapted enzyme Cold shock proteins Gene expression Low temperature Psychrophilic bacteria |
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