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.
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http://dx.doi.org/10.1007/s00792-002-0285-4 | DOI Listing |
Food Chem X
January 2025
Zhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
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Department of Mathematics and Statistics, Hazara University, Mansehra, Pakistan.
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Physics Centre of Minho and Porto Universities (CF-UM-UP) and LaPMET - Laboratory of Physics for Materials and Emergent Technologies, University of Minho, 4710-057 Braga, Portugal.
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Department of Physical Sciences, Indian Institute of Science Education and Research Mohali, Knowledge City, Sector 81, SAS Nagar, Manauli, 140306, India.
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