Abstract: Certain tRNA synthetases have developed highly accurate molecular machinery to discriminate their cognate amino acids. Those aaRSs achieve their goal via editing reaction in the Connective Polypeptide 1 (CP1). Recently mutagenesis studies have revealed the critical importance of residues in the CP1 domain for editing activity and X-ray structures have shown binding mode of noncognate amino acids in the editing domain. To pursue molecular mechanism for amino acid discrimination, molecular modeling studies were performed. Our results suggest that aaRS bind the noncognate amino acid more tightly than the cognate one. Finally, by comparing binding conformations of the amino acids in three systems, the amino acid binding mode was elucidated and a discrimination mechanism proposed. The results strongly reveal that the conserved threonines are responsible for amino acid discrimination. This is achieved through side chain interactions between T252 and T247/T248 as well as between those threonines and the incoming amino acids.
Abstract: The purpose of this study was to evaluate the tissue
composition and carcass muscularity of 32 legs of Ile de France
lambs fed with diets containing sunflower seeds and vitamin E, with
mean body weight of 15 kg, lodged in individual pens at 15 kg and
slaughtered at 32 kg of body weight. The treatments influenced
(P0,05) by the treatments. The
interaction of the sunflower and vitamin E was positive for bone total
weights and intermuscular fat.