Proteomic study of cold shock protein in Bacillus stearothermophilus P1: Comparison of temperature downshifts

Autor: Fu-Ming Pan, Supachok Sinchaikul, Boonyaras Sookkheo, Suree Phutrakul, Shui-Tein Chen
Rok vydání: 2002
Předmět:
Zdroj: PROTEOMICS. 2:1316-1324
ISSN: 1615-9861
1615-9853
DOI: 10.1002/1615-9861(200209)2:9<1316::aid-prot1316>3.0.co;2-0
Popis: The thermophilic bacterium Bacillus stearothermophilus P1 is unique in its ability to thrive in extreme environments such as high temperatures or high pH conditions. The study of cold shock response is very interesting and interpreted as a shock response to express the genes involved in synthesis of specific proteins. This study investigated the study of cold shock protein of B. stearothermophilus P1 when the cell culture temperature shifted from 65 degrees C to 37 degrees C and 25 degrees C. Cell growth at 37 degrees C weakly increased in the previous 3 h and then slowly decreased. In contrast, cell growth at 25 degrees C was slowly decreased. The protein contents after temperature downshifts were analyzed by proteomic techniques using protein chip and two-dimensional (2-D) electrophoresis that are highly effective and useful for protein separation and identification. The different proteins after a temperature decrease from 65 degrees C to 37 degrees C and 25 degrees C were expressed on 2-D gel patterns and the cold shock protein was detected in the acidic area with the isoelectric point and molecular mass approximately 4.5 and 7.3 kDa, respectively. The NH(2)-terminal sequence of a major cold shock protein from B. stearothermophilus P1 was MQRGKVKWFNNEKGFGFIEVEGGSD, similar to other cold shock proteins from Bacillus sp. up to 96% identity, but different from the other bacteria with homology less than 80% identity.
Databáze: OpenAIRE
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