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논문 기본 정보
- 자료유형
- 학술대회자료
- 저자정보
- 발행연도
- 2021.10
- 수록면
- 106 - 106 (1page)
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The dynamic changes in proteome profiles of Escherichia coli BL21(DE3), a widely used host for recombinant protein expression, were systematically monitored under stress conditions through 2-DE based quantitative proteomics - 1) disturbed redox balance, caused by dithiothreitol and 2-hydroxyethyl disulfide and 2) accelerated protein unfolding/misfolding, caused by guanidine hydrochloride and heat shock. Approximately 80 proteins including heat shock proteins/foldases, transcription/translation-related proteins, various metabolic enzymes, and other stress regulatory proteins were found to be notably upregulated in response to the stresses, among which 26 proteins were identified as new stress-responsive proteins. In particular, it is worthy of noting that the following proteins were dramatically (i.e. more than 2.5 fold compared to non-stress condition) upregulated: phosphotransferase enzyme IIA component (Crr), malate dehydrogenase (Mdh), spermidine/ putrescine-binding periplasmic protein (PotD), DNA-directed RNA Polymerase alpha-chain (RpoA), RNA polymerase sigma factor rpoS (RpoS), a FKBP-type peptidyl-prolyl cis-trans isomerse (SlyD), elongation factor Ts (Tsf), and a hypothetical protein YrhB, which are presumed to have high affinity for and thus closely interact with bacterial chaperones, leading to the upreg ... 전체 초록 보기
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