KRS1/YDR037W Summary Help

KRS1 BASIC INFORMATION

Standard Name KRS1
Systematic Name YDR037W
Alias GCD5
Feature Type ORF, Verified
Description Lysyl-tRNA synthetase (1 and see Summary Paragraph)
Name Description Lysyl (K) tRNA Synthetase
Gene Product Alias lysyl-tRNA synthetase 1
GO Annotations All KRS1 GO evidence and references
    View Computational GO annotations for KRS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All KRS1 Phenotype details and references
Large-scale survey
null
Interactions KRS1 All interactions details and references
50 total interaction(s) for 46 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 13
  • Biochemical Activity: 4
Genetic Interactions
  • Phenotypic Enhancement: 26
  • Phenotypic Suppression: 3
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1
Sequence Information
ChrIV:525438 to 527213 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2008-06-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1776 525438..527213 2008-06-05 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002444

KRS1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Localization Resources
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  • Phenotype Resources
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for KRS1

SUMMARY PARAGRAPH for KRS1

KRS1 encodes cytoplasmic lysyl-tRNA synthetase (1), the aminoacyl-tRNA synthetase specific for lysine. A second lysyl-tRNA synthetase, Msk1p, is localized to mitochondria. Both the cytoplasmic and mitochondrial enzymes are required for the import of nuclear encoded tRNA(lys)CUU into mitochondria (2).

In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (3, 4 and references therein).

Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (3, 4, 5 and references therein).

The expression of KRS1 is under general amino acid control and a mutant was initially characterized as a negative regulator of general control of amino acid biosynthesis (6, 1). Further research demonstrated that this Krs1p mutation results in a decrease in lysyl-tRNA concentrations, which initiates a response to amino acid starvation in the cell (7).

Last updated: 2008-07-14

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for KRS1]

1) Mirande M and Waller JP  (1988) The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein. J Biol Chem 263(34):18443-51
2) Tarassov I, et al.  (1995) Mitochondrial import of a cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases. EMBO J 14(14):3461-71
3) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
4) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
5) Eriani G, et al.  (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6
6) Greenberg ML, et al.  (1986) New positive and negative regulators for general control of amino acid biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol 6(5):1820-9
7) Lanker S, et al.  (1992) Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and transcriptional control mechanisms. Cell 70(4):647-57