Biomedical subjects
Publications and source records attributed to P Imbault.
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Chloroplastic and cytoplasmic valyl- and leucyl-tRNA synthetases purified from Euglena gracilis show a monomeric structure. The molecular weights of the two valyl-tRNA synthetases are identical (126,000) while those of the leucyl-tRNA synthetases are different (100 000 for the chloroplastic and 116 000 for the cytoplasmic enzyme). The tryptic maps and the amino acid compositions reveal differences between the chloroplastic valyl- and leucyl-tRNA synthetases and their cytoplasmic homologues. These results suggest that a chloroplastic aminoacyl-tRNA synthetase and its cytoplasmic counterpart are coded for by distinct genes.
Euglena gracilis chloroplast leucyl-tRNA synthetase was purified to homogeneity by a series of steps including ammonium sulfate precipitation and chromatography on hydroxylapatite, DEAE-cellulose, Sepharose 6B, phosphocellulose, and Blue Dextran-Sepharose. The purified enzyme exhibits a specific activity of 1233 units/mg of protein, which is one of the highest specific activities obtained for an aminoacyl-tRNA synthetase prepared from plant cells. The enzyme has an apparent Km value of 8 x 10(-6) M for L-leucine, 1.3 x 10(-4) M for ATP, and 1.3 x 10(-6) M for tRNALeu. Chloroplast leucyl-tRNA synthetase appears to be a monomeric enzyme with a molecular weight of 100 000. The amino acid composition of chloroplast leucyl-tRNA synthetase has been determined. It is the first reported for a chloroplast aminoacyl-tRNA synthetase, and it reveals a relatively large proportion of apolar residues, as in the case of prokaryotic aminoacyl-tRNA synthetases.
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When the growth rate of yeast cells is decreased (for instance by transferring the cells from a rich medium to a poor one, or when the cells enter the stationary phase, or when growth is inhibited by cycloheximide, or when valine is removed from the medium supporting growth of a valine-requiring mutant, or when a thermosensitive mutant is shifted to the non-permissive temperature) there is a decrease in the levels of the four aminoacyl-tRNA synthetases tested. Conversely, an increase in the growth rate is accompanied by an increase in the levels of the four enzymes. But when the growth rate is slowed down by decreasing the temperature of the medium, no effect on the levels of the aminoacyl-tRNA synthetases is observed. These results are consistent with the concept of "metabolic regulation" proposed by Parker and neidhardt.
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