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Literature summary for 6.1.1.6 extracted from

  • Remion, A.; Khoder-Agha, F.; Cornu, D.; Argentini, M.; Redeker, V.; Mirande, M.
    Identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex the case of lysyl-tRNA synthetase and the scaffold protein p38 (2016), FEBS open bio, 6, 696-706 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of enzyme LysRS in Escherichia coli strain BL21(DE3) that also contains pEVOL-p-benzoyl-L-phenylalanine (Bpa) expressing the orthogonal suppression system, namely Methanococcus jannaschii tRNATyr,CUA, an amber suppressor tRNA derived from Methanococcus jannaschii tRNATyr, and Methanococcus jannaschii TyrRSBpa a mutant of Methanococcus jannaschii tyrosyl-tRNA synthetase that specifically aminoacylates Methanococcus jannaschii tRNATyr,CUA with Bpa Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information incorporation of the non-natural, photo-cross-linkable amino acid p-benzoyl-L-phenylalanine (Bpa) at 27 discrete positions within the catalytic domain of LysRS. Among the 27 distinct LysRS mutants, only those with Bpa inserted in place of Lys356 or His364 are cross-linked with p38, the scaffold protein of the -aminoacyl-tRNA synthetase complex (MSC) Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Homo sapiens 5737
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q15046
-
-

Subunits

Subunits Comment Organism
More identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex including lysyl-tRNA synthetase and the scaffold protein p38, overview Homo sapiens

Synonyms

Synonyms Comment Organism
cytoplasmic lysyl-tRNA synthetase
-
Homo sapiens
KARS
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Homo sapiens
LysRS
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Homo sapiens
Lysyl-tRNA synthetase
-
Homo sapiens

General Information

General Information Comment Organism
additional information human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via its N-terminal region, LysRS-p38 interaction analysis, Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, overview Homo sapiens
physiological function in addition to its translational function when associated to the a multi-aminoacyl-tRNA synthetase complex (MSC), LysRS is also recruited in nontranslational roles after dissociation from the MSC. The balance between its MSC-associated and MSC-dissociated states is essential to regulate the functions of LysRS in cellular homeostasis Homo sapiens