PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 10205299

Dimer formation by tRNAs.

N S Kholod
View original source ↗Export metadata ↓

Abstract

Available data on formation of dimers and other oligomers by "mature" tRNAs and the transcripts of their genes show that the dimers may be formed in vitro during the purification of individual tRNAs as well as on heating and subsequent cooling of tRNA preparations. The functional activity of dimers varies for different tRNAs. Structural analysis of tRNAs that are able or unable to form dimers suggests the importance of the hairpin melting temperature for dimer formation. Pathways of dimer formation and specific structural features of tRNA dimers are discussed.

Explore related subjects

Amino Acyl-tRNA SynthetasesBase SequenceDimerizationDrug StabilityMagnesiumMolecular Sequence DataNucleic Acid ConformationNucleic Acid DenaturationRNA, BacterialRNA, FungalRNA, TransferRNA, Transfer, AlaRNA, Transfer, TyrTemperatureJournal ArticleResearch Support, Non-U.S. Gov'tReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

N S Kholod. 1999. Dimer formation by tRNAs.. https://pubmed.ncbi.nlm.nih.gov/10205299/

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

KEEP EXPLORING

Related citations

PubMed2001

Active site of an aminoacyl-tRNA synthetase dissected by energy-transfer-dependent fluorescence.

Aminoacyl-tRNA synthetases establish the rules of the genetic code by catalyzing attachment of amino acids to specific transfer RNAs (tRNAs) that bear the anticodon triplets of the code. Each of the 20 amino acids has its own distinct aminoacyl-tRNA synthetase. Here we use energy-transfer-dependent fluorescence from the nucleotide probe N-methylanthraniloyl dATP (mdATP) to investigate the active site of a specific aminoacyl-tRNA synthetase. Interaction of the enzyme with the cognate amino acid and formation of the aminoacyl adenylate intermediate were detected. In addition to providing a convenient tool to characterize enzymatic parameters, the probe allowed investigation of the role of conserved residues within the active site. Specifically, a residue that is critical for binding could be distinguished from one that is important for the transition state of adenylate formation. Amino acid binding and adenylate synthesis by two other aminoacyl-tRNA synthetases was also investigated with mdATP. Thus, a key step in the synthesis of aminoacyl-tRNA can in general be dissected with this probe.

Amino Acyl-tRNA Synthetases↗
PubMed2001

A cofactor of tRNA synthetase, p43, is secreted to up-regulate proinflammatory genes.

An auxiliary factor of mammalian multi-aminoacyl-tRNA synthetases, p43, is thought to be a precursor of endothelial monocyte-activating polypeptide II (EMAP II) that triggers proinflammation in leukocytes and macrophages. In the present work, however, we have shown that p43 itself is specifically secreted from intact mammalian cells, while EMAP II is released only when the cells are disrupted. Secretion of p43 was also observed when its expression was increased. These results suggest that p43 itself should be a real cytokine secreted by an active mechanism. To determine the cytokine activity and active domain of p43, we investigated tumor necrosis factor (TNF) and interleukin-8 (IL-8) production from human monocytic THP-1 cells treated with various p43 deletion mutants. The full length of p43 showed higher cytokine activity than EMAP II, further supporting p43 as the active cytokine. p43 was also shown to activate MAPKs and NFkappaB, and to induce cytokines and chemokines such as TNF, IL-8, MCP-1, MIP-1alpha, MIP-1beta, MIP-2alpha, IL-1beta, and RANTES. Interestingly, the high level of p43 was observed in the foam cells of atherosclerotic lesions. Therefore, p43 could be a novel mediator of atherosclerosis development as well as other inflammation-related diseases.

Amino Acyl-tRNA Synthetases↗