GRS2/YPR081C Summary Help

Standard Name GRS2 1
Systematic Name YPR081C
Feature Type ORF, Verified
Description Glycine-tRNA synthetase, not expressed under normal growth conditions; expression is induced under heat, oxidative, pH, or ethanol stress conditions; more stable than the major glycine-tRNA synthetase Grs1p at 37 deg C; GRS2 has a paralog, GRS1, that arose from the whole genome duplication (1, 2, 3, 4 and see Summary Paragraph)
Name Description Glycyl-tRNA Synthase 1
Chromosomal Location
ChrXVI:703970 to 702114 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All GRS2 GO evidence and references
  View Computational GO annotations for GRS2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
39 total interaction(s) for 39 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Two-hybrid: 5

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 21
  • Positive Genetic: 7

Resources
Expression Summary
histogram
Resources
Length (a.a.) 618
Molecular Weight (Da) 71,018
Isoelectric Point (pI) 7.5
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:703970 to 702114 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1857 703970..702114 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006285
SUMMARY PARAGRAPH for GRS2

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 (5, 6 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 (5, 6, 7 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for GRS2
1) Turner RJ, et al.  (2000) One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions. J Biol Chem 275(36):27681-8
2) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
3) Chen SJ, et al.  (2011) Rescuing a dysfunctional homologue of a yeast glycyl-tRNA synthetase gene. ACS Chem Biol 6(11):1182-7
4) Chen SJ, et al.  (2012) Saccharomyces cerevisiae Possesses a Stress-Inducible Glycyl-tRNA Synthetase Gene. PLoS One 7(3):e33363
5) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
6) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
7) 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