Do Prokaryotes Have More Kinetically Stable Proteins Than Eukaryotic Organisms?

Abstract

Upon folding, some proteins become conformationally trapped, presumably to protect against aggregation or premature degradation. To probe the occurrence of this property, known as kinetic stability, we used a diagonal two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis method to probe biologically diverse organisms. The results show that kinetic stability is prevalent in prokaryotes, especially thermophiles, but uncommon in eukaryotic organisms, thereby suggesting that this property might be crucial for the adaptation and survival of less complex prokaryotic organisms.

Copper, zinc superoxide dismutase from Caragana jubata : A thermostable enzyme that functions under a broad pH and temperature window

“…38 The kinetic stability of proteins may be related to evolution. 40 The thermal stability of enzymes is a desirable feature for industrial applications that require high temperatures to develop products. 41 In species adapted to different thermal regimes, the kinetic properties of enzymes are typically correlated with environmental temperatures, but the correlation between adaptation temperature and enzyme thermal stability is less clear.…”

“…The decreased rate of local and global unfolding of kinetically stable proteins accounts for their resistance to SDS-induced denaturation. 40 The inability of SDS to dissociate Cj-Cu, Zn SOD indicated that the enzyme was resistant to subunit dissociation (Fig. S6) in the presence of SDS 38,39 and is thus kinetically stable.…”

Proteomics Analysis of Kinetically Stable Proteins

“…3. D2D SDS-PAGE assay for detecting KSPs ( (Xia, et al, 2007;Xia, Zhang, Solina, Barquera, & Colon, 2010). After 1D SDS-PAGE, the gel strip is excised and incubated in boiling SDS.…”

“…Therefore, we studied the cell lysates of the thermophilic bacteria Thermus thermophilus and Thermus aquaticus, and the archaea Sulfolobus acidocaldarius, which grow at optimal temperatures of 65, 70, and 80°C, respectively (Xia, Zhang, Solina, Barquera, & Colon, 2010) These thermophiles exhibited high number of SDS-resistant (i.e. KSPs) proteins (Fig.…”

“…7. D2D SDS-PAGE of the lysate of various organisms to probe the extent of kinetically stable proteins present (Xia, Zhang, Solina, Barquera, & Colon, 2010). (a) Thermophilic prokaryotes (T. thermophilus, S. acidoldarius, and T. aquaticus) exhibited significantly more spots migrating to the left of the diagonal than (b) mesophilic prokaryotes (E. coli, V. cholerae, and B. subtilis).…”