Abstract
The proteomes expressed at 4°C and 18°C by the psychrophilic Antarctic bacterium Pseudoalteromonas haloplanktis were compared using two-dimensional differential in-gel electrophoresis with special reference to proteins repressed by low temperatures. Remarkably, the major cold-repressed proteins, almost undetectable at 4°C, were heat shock proteins involved in folding assistance.
Publication types
- Research Support, Non-U.S. Gov't
MeSH terms
- Antarctic Regions
- Bacterial Proteins / analysis*
- Cold Temperature
- Electrophoresis, Gel, Two-Dimensional
- Environmental Microbiology
- Gene Expression Regulation, Bacterial*
- Proteome / analysis*
- Pseudoalteromonas / genetics*
- Pseudoalteromonas / isolation & purification
- Pseudoalteromonas / metabolism*
- Pseudoalteromonas / radiation effects
Substances
- Bacterial Proteins
- Proteome