cd04322

LysRS_N

CDD entry
Member databaseCDD
CDD typedomain
Short nameLysRS_N
SetRPA_2b-aaRSs_OBF_like

Description

LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging.
[14, 7, 15, 2, 5, 13, 16, 9, 20, 4, 17, 8, 12, 22, 1, 3, 18, 21, 11, 19, 6, 10]

References

1.In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase. Kovaleski BJ, Kennedy R, Hong MK, Datta SA, Kleiman L, Rein A, Musier-Forsyth K. J Biol Chem 281, 19449-56, (2006). PMID: 16702215

2.Properties of the lysyl-tRNA synthetase gene and product from the extreme thermophile Thermus thermophilus. Chen J, Brevet A, Lapadat-Tapolsky M, Blanquet S, Plateau P. J Bacteriol 176, 2699-705, (1994). PMID: 8169220

3.The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript. Tolkunova E, Park H, Xia J, King MP, Davidson E. J Biol Chem 275, 35063-9, (2000). PMID: 10952987

4.The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein. Mirande M, Waller JP. J Biol Chem 263, 18443-51, (1988). PMID: 2903861

5.Comparison of the enzymatic properties of the two Escherichia coli lysyl-tRNA synthetase species. Brevet A, Chen J, Leveque F, Blanquet S, Plateau P. J Biol Chem 270, 14439-44, (1995). PMID: 7782306

6.Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Nature 347, 203-6, (1990). View articlePMID: 2203971

7.Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. Biochemistry 39, 12853-61, (2000). View articlePMID: 11041850

8.Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P. J Biol Chem 272, 22809-16, (1997). PMID: 9278442

9.Crystallization and preliminary diffraction studies of Escherichia coli lysyl-tRNA synthetase (LysU). Onesti S, Theoclitou ME, Pernilla E, Wittung L, Miller AD, Plateau P, Blanquet S, Brick P. J Mol Biol 243, 123-5, (1994). PMID: 7932734

10.Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Woese CR, Olsen GJ, Ibba M, Soll D. Microbiol. Mol. Biol. Rev. 64, 202-36, (2000). View articlePMID: 10704480

11.Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update. Cusack S. Biochimie 75, 1077-81, (1993). View articlePMID: 8199242

12.A root-specific iron-regulated gene of tomato encodes a lysyl-tRNA-synthetase-like protein. Giritch A, Herbik A, Balzer HJ, Ganal M, Stephan UW, Baumlein H. Eur J Biochem 244, 310-7, (1997). PMID: 9118995

13.The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli. Onesti S, Miller AD, Brick P. Structure 3, 163-76, (1995). View articlePMID: 7735833

14.Lysyl-tRNA synthetase. Freist W, Gauss DH. Biol Chem Hoppe Seyler 376, 451-72, (1995). PMID: 7576245

15.Characterization of a Mycoplasma hominis gene encoding lysyl-tRNA synthetase (LysRS). Ozkokmen D, Birkelund S, Christiansen G. FEMS Microbiol Lett 116, 277-82, (1994). PMID: 8181699

16.Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction. Desogus G, Todone F, Brick P, Onesti S. Biochemistry 39, 8418-25, (2000). View articlePMID: 10913247

17.Mitochondrial import of a cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases. Tarassov I, Entelis N, Martin RP. EMBO J 14, 3461-71, (1995). PMID: 7628447

18.Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Park SG, Kim HJ, Min YH, Choi EC, Shin YK, Park BJ, Lee SW, Kim S. Proc Natl Acad Sci U S A 102, 6356-61, (2005). PMID: 15851690

19.Aminoacyl-tRNA synthetases database. Szymanski M, Deniziak MA, Barciszewski J. Nucleic Acids Res 29, 288-90, (2001). PMID: 11125115

20.Lysyl-tRNA synthetase gene of Campylobacter jejuni. Chan VL, Bingham HL. J Bacteriol 174, 695-701, (1992). PMID: 1732205

21.Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Cusack S, Hartlein M, Leberman R. Nucleic Acids Res. 19, 3489-98, (1991). View articlePMID: 1852601

22.Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and transcriptional control mechanisms. Lanker S, Bushman JL, Hinnebusch AG, Trachsel H, Mueller PP. Cell 70, 647-57, (1992). PMID: 1505029

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