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Kars  -  lysyl-tRNA synthetase

Mus musculus

Synonyms: AA589550, AL024334, AL033315, AL033367, D8Ertd698e, ...
 
 
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Disease relevance of Kars

  • LysRS and TrpRS are present in HIV-1 and RSV at approximately 25 and 12 molecules/virion, respectively [1].
 

High impact information on Kars

  • We have also shown that Ap4A, an endogenous molecule consisting of two adenosine linked by four phosphate which is known to be synthesized by LysRS, is accumulated intracellularily above 700 microM in IgE-Ag-activated mast cells, binds to Hint, liberates MITF, and thus leads to the activation of MITF-dependent gene expression [2].
  • Here, we show for the first time that LysRS associates with another transcription factor, USF2, which unlike MITF, is ubiquitously expressed in eukaryotic cells [3].
  • The distinctions between tRNALys2 and tRNALys4 may be part of significant cellular roles as illustrated by the differential effects of these isoacceptors on the synthesis by lysyl-tRNA synthetase of diadenosine-5',5'''-P1,P4-tetraphosphate, a putative signal in DNA replication [4].
  • In contrast, the specific activity of lysyl-tRNA synthetase from the Balb/3T3 complex was 50% higher than that of the KA31 complex. tRNALys obtained from the complexes of Balb/3T3 and KA31 was fractionated into isoacceptors on columns of RPC-5 [5].
 

Anatomical context of Kars

  • Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcepsilonRI-activated mast cells [3].
 

Analytical, diagnostic and therapeutic context of Kars

  • For Lysyl tRNA synthetase, NET1, MTMR1 and hSec8, binding to TIP-15 was confirmed by co-immunoprecipitation experiments performed with the extracts of transfected COS7 cells [6].

References

  1. Retrovirus-specific packaging of aminoacyl-tRNA synthetases with cognate primer tRNAs. Cen, S., Javanbakht, H., Kim, S., Shiba, K., Craven, R., Rein, A., Ewalt, K., Schimmel, P., Musier-Forsyth, K., Kleiman, L. J. Virol. (2002) [Pubmed]
  2. The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Lee, Y.N., Nechushtan, H., Figov, N., Razin, E. Immunity (2004) [Pubmed]
  3. Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcepsilonRI-activated mast cells. Lee, Y.N., Razin, E. Mol. Cell. Biol. (2005) [Pubmed]
  4. Structural relationship between tRNALys2 and tRNALys4 from mouse lymphoma cells. Hayenga, K., Hedgcoth, C., Harrison, M., Lin, V.K., Ortwerth, B.J. Mol. Cell. Biochem. (1986) [Pubmed]
  5. Comparison of complexes containing lysyl-tRNA synthetase from normal and virus-transformed cells. Thomas, K., Scheets, K., Allen, S., Hedgcoth, C. Can. J. Biochem. (1982) [Pubmed]
  6. Identification of functional PDZ domain binding sites in several human proteins. Fabre, S., Reynaud, C., Jalinot, P. Mol. Biol. Rep. (2000) [Pubmed]
 
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