Thermal stability of aminoacyl-tRNAs in aqueous solutions.
Life in hot environments poses certain constraints on the metabolism of thermophilic organisms. Many universal metabolic intermediates are quite labile compounds, and without protection will rapidly decompose at elevated temperatures. Among these are aminoacyl-tRNAs that are necessarily formed upon functioning of the translation apparatus. Aminoacyl-tRNAs are known to be hydrolyzed rapidly even at moderate temperatures under mild alkaline conditions. We studied the thermal stability of phenylalanyl- and alanyl-tRNA in aqueous solutions in order to evaluate a potential threat posed by high temperatures to these components of the translation machinery of thermophiles. Specific second-order rate constants of the aminoacyl-tRNA hydrolysis reaction were determined in the range 20 degrees -80 degrees C. The activation energy of phenylalanyl- and alanyl-tRNA hydrolysis was found to be about 42 and 23 kJ/mol, respectively. The calculated half-lives of aminoacyl-tRNAs at sub-80 degrees C temperatures vary from several seconds to several dozens of seconds at near-neutral pH. The possible mechanisms counteracting the observed thermolability of aminoacyl-tRNAs in vivo are discussed.
Stepanov
Victor G
VG
Institute of Molecular and Structural Biology, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.
Nyborg
Jens
J
D004355:Drug Stability; D006207:Half-Life; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry*; D012996:Solutions; D014867:Water
D012346:RNA, Transfer, Amino Acyl; D012996:Solutions; D014867:Water