title: Proteomic analysis of heat-stable proteins in Escherichia coli.
abstract: Some proteins of E. coli are stable at temperatures significantly higher than 49 degrees C, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E. coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GroEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures.
authors.affiliation: Department of Bioinformatics and Life Science, Soongsil University, Seoul, Korea.
authors.forename: Soonbok
authors.initials: S
authors.lastname: Kwon
authors.forename: Yuna
authors.initials: Y
authors.lastname: Jung
authors.forename: Dongbin
authors.initials: D
authors.lastname: Lim
mesh_terms: D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006358:Hot Temperature; D011489:Protein Denaturation; D020543:Proteome / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D029968:Escherichia coli Proteins; D020543:Proteome