KRS1/YDR037W Summary Help

Standard Name KRS1 1
Systematic Name YDR037W
Alias GCD5
Feature Type ORF, Verified
Description Lysyl-tRNA synthetase (1 and see Summary Paragraph)
Name Description Lysyl (K) tRNA Synthetase 1
Gene Product Alias lysyl-tRNA synthetase 1
Chromosomal Location
ChrIV:525440 to 527215 | ORF Map | GBrowse
Gene Ontology 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
Regulators 6 genes
Large-scale survey
reduction of function
102 total interaction(s) for 89 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-RNA: 5
  • Biochemical Activity: 4

Genetic Interactions
  • Negative Genetic: 57
  • Phenotypic Enhancement: 1
  • Positive Genetic: 10
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 3
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 591
Molecular Weight (Da) 67,958
Isoelectric Point (pI) 6.04
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:525440 to 527215 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1776 525440..527215 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002444

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).

About aminoacyl-tRNA synthetases...

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 Contact SGD

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