Comparative analysis of DNA-binding proteins between thermophilic and mesophilic bacteria.
Thermophilic bacteria are one of the most attractive forms of life, and their adaptation mechanisms to elevated temperatures have been extensively studied over the years. Thermal adaptations of cell components such as proteins and RNA are well studied, but adaptations of interactions between these components must be also vital for the thermophiles. Protein-DNA interactions play crucial roles in the cell, but little is known about their thermal adaptations. In this study, we analyzed DNA-binding proteins from thermophilic bacteria. Comparison of amino acid compositions at the DNA-binding interfaces between thermophiles and their mesophilic close relatives revealed several commonalities between phylogenetically unrelated organisms. Advantages and limitations of our methods will be also discussed.
Fujita
Masashi
M
Bioinformatics Center, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan. fujita@kuicr.kyoto-u.ac.jp
Kanehisa
Minoru
M
D000222:Adaptation, Physiological; D000596:Amino Acids / Q000737:chemistry*; D001105:Archaea / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics; D019295:Computational Biology; D004268:DNA-Binding Proteins / Q000032:analysis* / Q000235:genetics; D020543:Proteome / Q000737:chemistry; D013045:Species Specificity; D013696:Temperature
D000596:Amino Acids; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D020543:Proteome