PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7504246

Discrimination among E. coli tRNAs with a long variable arm.

H Asahara·H Himeno·K Tamura·N Nameki·T Hasegawa·M Shimizu
View original source ↗Export metadata ↓

Abstract

In E. coli, tRNA(Ser), tRNA(Leu) and tRNA(Tyr) have a long variable arm composed of more than ten nucleotides (class II tRNAs). In order to study how leucyl- and seryl-tRNA synthetase discriminate their cognate tRNA isoacceptors from the other class II tRNAs, kinetic parameters of various mutated class II tRNA transcripts with leucyl- and seryl-tRNA synthetase were determined. Leucyl-tRNA synthetase recognizes A73 and A14 or its vicinity. Seryl-tRNA synthetase recognizes the long variable arm base-nonspecifically. C2-G71 in the acceptor stem functions as a negative identity element against seryl-tRNA synthetase. Difference in the tertiary structure among class II tRNA molecules plays a crucial role in discrimination by these two synthetases.

Explore related subjects

AcylationEscherichia coliKineticsLeucine-tRNA LigaseMutationNucleic Acid ConformationRNA, BacterialRNA, Transfer, SerRNA, Transfer, TyrSerine-tRNA LigaseJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

H Asahara, H Himeno, K Tamura, N Nameki, T Hasegawa, M Shimizu. 1993. Discrimination among E. coli tRNAs with a long variable arm.. https://pubmed.ncbi.nlm.nih.gov/7504246/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

A quantum mechanics/molecular mechanics study of the reaction mechanism of the hepatitis C virus NS3 protease with the NS5A/5B substrate.

Combined quantum mechanics and molecular mechanics (QM/MM) calculations were carried out to characterize the reaction mechanism of the NS3 protease with its preferred substrate (NS5A/5B). The main purpose of this study was to locate the barrier states and intermediates along the distinguished coordinate path (DCP) involved in this process. These structures, and in particular the one corresponding to the first barrier state and intermediate (B1 and I1), could be a starting point for the synthesis of inhibitors of this protease, which could be used to treat hepatitis C. The two first steps of the reaction mechanism were studied, i.e., the acylation step and the breaking of the peptide bond. The first step takes place through a tetracoordinated intermediate, as suggested from previous works on other Serine proteases. The importance of the different amino acid residues was also considered (perturbation study where the MM charges of each residue were set to zero independently). The residues of the oxyanion hole were confirmed as the most important for the electrostatic stabilization of the tetracoordinate intermediate. Moreover, the role of other residues, e.g., Arg-155 and Asp-79, was also explained.

Acylation↗
PubMed2007

Dual lipid modification of Arabidopsis Ggamma-subunits is required for efficient plasma membrane targeting.

Posttranslational lipid modifications are important for proper localization of many proteins in eukaryotic cells. However, the functional interrelationships between lipid modification processes in plants remain unclear. Here we demonstrate that the two heterotrimeric G-protein gamma-subunits from Arabidopsis (Arabidopsis thaliana), AGG1 and AGG2, are prenylated, and AGG2 is S-acylated. In wild type, enhanced yellow fluorescent protein-fused AGG1 and AGG2 are associated with plasma membranes, with AGG1 associated with internal membranes as well. Both can be prenylated by either protein geranylgeranyltransferase I (PGGT-I) or protein farnesyltransferase (PFT). Their membrane localization is intact in mutants lacking PFT activity and largely intact in mutants lacking PGGT-I activity but is disrupted in mutants lacking both PFT and PGGT-I activity. Unlike in mammals, Arabidopsis Ggammas do not rely on functional Galpha for membrane targeting. Mutation of the sixth to last cysteine, the putative S-acylation acceptor site, causes a dramatic change in AGG2 but not AGG1 localization pattern, suggesting S-acylation serves as an important additional signal for AGG2 to be targeted to the plasma membrane. Domain-swapping experiments suggest that a short charged sequence at the AGG2 C terminus contributes to AGG2's efficient membrane targeting compared to AGG1. Our data show the large degree to which PFT and PGGT-I can compensate for each other in plants and suggest that differential lipid modification plays an important regulatory role in plant protein localization.

Acylation↗
PubMed2007

New bradykinin analogues acylated on the N-terminus: effect on rat uterus and blood pressure.

Our previous studies suggested that acylation of the N-terminus of several known B2 antagonists with various kinds of bulky acyl groups consistently improved their antagonistic potency in rat blood pressure assay. On the other hand, our earlier observations also seemed to suggest that the effects of acylation on the contractility of isolated rat uterus depended substantially on the chemical character of the acyl group, as we observed that this modification might either change the range of antagonism or even transform it into agonism. Bearing all this in mind, we decided to synthesize seven new analogues of bradykinin by N-terminal acylation with various acyl groups of a moderately potent B2 antagonist, previously synthesized by Stewart's group, D-Arg-Arg-Pro-Hyp-Gly-Thr-Ser-D-Phe-Thi-Arg. The analogues were tested in vitro for their blood pressure-lowering and uterotonic activities. The modifications either preserved or increased the antagonistic potency in the rat blood pressure test. On the other hand, all seven substituents negatively influenced the interaction with the rat uterine receptors. Our results may be helpful for designing new B2 agonists and antagonists.

Acylation↗