Mutual conformational changes of tryptophanyl-tRNA synthetase and tRNATrp in the course of their specific interaction

tRNATrp (beef, yeast) is capable of accelerating limited tryptic hydrolysis of the N-terminal part in the polypeptide chains of dimeric beef pancreas tryptophanyl-tRNA synthetase; it can also eliminate the protective effect of tryptophanyl adenylate on the enzyme proteolysis. The effect of tRNA on the proteolysis is manifested even when the 3'-CCA terminus is removed. It has been concluded that the conformation of the synthetase changes when it forms a complex with tRNATrp. Yeast tRNATrp lacking the 3'-half of the acceptor stem can still interact with the synthetase and, to certain extent, induces changes in the conformation of the latter. The susceptibility of single-stranded and double-stranded regions of tRNATrp to cleavage with endonucleases has been studied, and the results are indicative of the fact that, regardless of considerable differences in the nucleotide sequence of yeast and beef tRNATrp, their three-dimensional structures are similar. This fact is consistent with the finding that parameters for the interaction of these tRNAsTrp with beef tryptophanyl-tRNA synthetase are rather close. The three-dimensional structure of tRNATrp is altered when the enzyme forms a complex with it, as seen from (a) a change in the circular dichroic spectrum and (b) an elevated susceptibility of the anticodon and, apparently, acceptor stems to cleavage with nuclease. The conversion of exposed cytidine residues in tRNATrp into uridine residues results in a loss of the acceptor activity; the capability to accelerate limited tryptic hydrolysis of tryptophanyl-tRNA synthetase is also lost although the enzyme-substrate complex, as seen from circular dichroic spectra, can still be formed. The conversion of cytosine in the anticodon stem into uracil modifies the conformation of the anticodon stem. The anticodon arm (including the anticodon) and the acceptor stem play an essential role in the interaction between tRNATrp and tryptophanyl-tRNA synthetase.     

Chilling-induced Lipid Hydrolysis in the Oil Palm (Elaeis guineensis) Mesocarp

Oil palm fruits exposed to temperatures of 15 °C and belowshowed a significant increase in free fatty acid (FFA) contentin the mesocarp. This effect was most pronounced in fruits exposedto 5 °C when FFA levels exceeding 70% of the total oil wereobserved. The increase in FFA was accompanied by an increasein lipid-soluble phosphorus levels and a decrease in carotenecontent. Chilling did not have an effect on palm kernel oil.The results suggest the activation of a lipase in the mesocarpby low temperature stress. Key words: Lipase, oil palm, free fatty acid     

Eukaryotic tryptophanyl-tRNA synthetase acquires affinity to high molecular weight RNA after limited proteolysis

It is shown that the native tryptophanyl-tRNA synthetase (Mr 2X60 kDa) isolated from bovine pancreas does not interact with high-molecular weight RNAs (E. coli rRNAs). The enzyme acquires the affinity for high-molecular weight RNAs after the cleavage of the 20 kDa fragment from each of the subunits upon digestion by protease. The possible functional significance of the discovered phenomenon is discussed.