Proteins Involved in Cold-adaptation
Kazuaki Yoshimune, Jun Kawamoto and Tatsuo Kurihara
from: Cold-Adapted Microorganisms (Edited by: Isao Yumoto). Caister Academic Press, U.K. (2013)
This chapter primarily describes cold shock proteins (CSPs), which are induced in response to temperature downshift in both psychrophiles and mesophiles. These proteins are important for various cellular processes, including transcription, translation, protein synthesis and folding, and membrane functions, to maintain their viability under cold conditions. Here, the CSPs in psychrophilic and mesophilic microorganisms are represented on the basis of the results of proteome analyses. In particular, CSPs that were isolated from the Antarctic psychrophile Shewanella livingstonensis Ac10 are described in detail. A number of microorganisms induce molecular chaperones in response to the cold, although the majority of chaperones are induced as a result of heat shock. Chaperones with peptidyl prolyl cis-trans isomerase activity are often induced by cold to accelerate protein folding by interconverting the cis and trans isomers of proline imidic peptide bonds, and these cold shock chaperones are also discribed here. Cold adapted proteins often have higher flexibility as compared to mesophilic proteins. The features of cold adapted proteins are briefly described. Finally, the production of recombinant proteins in psychrophiles is shown to suggest a future application of psychrophiles read more ...