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Literature summary for 6.1.1.6 extracted from
- Shiga toxins trigger the secretion of lysyl-tRNA synthetase to enhance proinflammatory responses (2016), J. Microbiol. Biotechnol., 26, 432-439 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene KARS, recombinant expression of Strep-tagged enzyme in 293-F cells | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | introduction of a Watson-Crick base pair (G69A) into each pneumococcal tRNALys isoacceptor results in an approximately 3fold increase in lysylation activity by LysRS compared to wild-type tRNAs. The overall mischarging profile of pneumococcal LysRS remains the same with both the wild-type and the G69A tRNALys transcripts, but the yield of Ala-tRNALys produced is increased by approximately 2fold for the TTT G69A transcript and 3fold for the CTT G69A transcript in comparison to the equivalent wild-type species | Streptococcus pneumoniae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Homo sapiens | 5829 | - |
| extracellular | dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex in human macrophage-like differentiated THP-1 cells and its subsequent secretion, can be triggered by Shiga toxins | Homo sapiens | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Homo sapiens |  |
| Mg2+ | required | Streptococcus pneumoniae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-lysine + tRNALys | Homo sapiens | - |
AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| ATP + L-lysine + tRNALys | Streptococcus pneumoniae | - |
AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| ATP + L-lysine + tRNALys | Streptococcus pneumoniae D39 / NCTC 7466 | - |
AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| additional information | Streptococcus pneumoniae | pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism | ? | - |
? | |
| additional information | Streptococcus pneumoniae D39 / NCTC 7466 | pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Streptococcus pneumoniae | Q04LI2 | - |
- |
| Streptococcus pneumoniae D39 / NCTC 7466 | Q04LI2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant Strep-tagged enzyme from 293-F cells by affinity chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| macrophage | - |
Homo sapiens | - |
| THP-1 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-lysine + tRNALys | - |
Homo sapiens | AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| ATP + L-lysine + tRNALys | - |
Streptococcus pneumoniae | AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| ATP + L-lysine + tRNALys | - |
Streptococcus pneumoniae D39 / NCTC 7466 | AMP + diphosphate + L-lysyl-tRNALys | - |
? | |
| additional information | pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism | Streptococcus pneumoniae | ? | - |
? | |
| additional information | analysis of the aminoacylation profiles of class II lysyl-tRNA synthetase (LysRS) | Streptococcus pneumoniae | ? | - |
? | |
| additional information | pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism | Streptococcus pneumoniae D39 / NCTC 7466 | ? | - |
? | |
| additional information | analysis of the aminoacylation profiles of class II lysyl-tRNA synthetase (LysRS) | Streptococcus pneumoniae D39 / NCTC 7466 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| class II lysyl-tRNA synthetase | - |
Streptococcus pneumoniae |
| KRS | - |
Homo sapiens |
| LysRS | - |
Streptococcus pneumoniae |
| lysS | - |
Streptococcus pneumoniae |
| Lysyl-tRNA synthetase | - |
Homo sapiens |
| Lysyl-tRNA synthetase | - |
Streptococcus pneumoniae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Homo sapiens | |
| ATP | - |
Streptococcus pneumoniae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the class II amino acyl-tRNA synthetases (aaRS) | Streptococcus pneumoniae |
| metabolism | Shiga toxins trigger the dissociation and secretion of KRS from the multi-aminoacyl-tRNA synthetase complex (MSC) in toxin-sensitive human macrophage-like D-THP-1 cells to enhance proinflammatory responses | Homo sapiens |
| physiological function | aminoacyl-tRNA synthetases provide the first step in protein synthesis quality control by discriminating cognate from noncognate amino acid and tRNA substrates. While substrate specificity is enhanced in many instances by cis- and transediting pathways, it has been revealed that in organisms such as Streptococcus pneumoniae some aminoacyl tRNA synthetases display significant tRNA mischarging activity. Pneumococcal LysRS misaminoacylates tRNALys with Ala and to a lesser extent Thr and Ser, with mischarging efficiency modulated by the presence of an unusual U4:G69 wobble pair in the acceptor stems of both pneumococcal tRNALys isoacceptors. Addition of the trans-editing factor MurM, which also functions in peptidoglycan synthesis, reduces Ala-tRNALys production by LysRS, providing evidence for cross talk between the protein synthesis and cell wall biogenesis pathways. Mischarging of tRNALys by AlaRS is also observed, and this provides additional potential MurM substrates. Adaptive misaminoacylation may contribute significantly to the viability of this pathogen during amino acid starvation. In the absence of efficient pre- and/or posttransfer editing mechanisms, the distorted region in the acceptor stem of tRNALys is able to reduce the overall mischarging capacity of pneumococcal LysRS, with an accompanying loss in cognate charging | Streptococcus pneumoniae |
| physiological function | Shiga toxins (Stxs) produced by Shiga toxin-producing Escherichia coli (STEC) strains are major virulence factors that cause fatal systemic complications, such as hemolytic uremic syndrome and disruption of the central nervous system. Enzymatically active Stxs trigger the dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex (MSC) in human macrophage-like differentiated THP-1 cells and its subsequent secretion. The secreted KRS acts to increase the production of proinflammatory cytokines and chemokines. Thus, KRS may be one of the key factors that mediate transduction of inflammatory signals in the STEC-infected host | Homo sapiens |
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