GRS1/YBR121C Summary Help

Standard Name GRS1 1
Systematic Name YBR121C
Feature Type ORF, Verified
Description Cytoplasmic and mitochondrial glycyl-tRNA synthase; ligates glycine to the cognate anticodon-bearing tRNA; transcription termination factor that may interact with the 3'-end of pre-mRNA to promote 3'-end formation; GRS1 has a paralog, GRS2, that arose from the whole genome duplication (1, 2, 3 and see Summary Paragraph)
Name Description Glycyl-tRNA Synthase 1
Gene Product Alias glycyl-tRNA synthetase 1
Chromosomal Location
ChrII:483367 to 481364 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All GRS1 GO evidence and references
  View Computational GO annotations for GRS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 6 genes
Resources
Classical genetics
conditional
reduction of function
Large-scale survey
conditional
null
overexpression
reduction of function
Resources
51 total interaction(s) for 42 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 22
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 1
  • PCA: 3

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 7
  • Positive Genetic: 2
  • Synthetic Growth Defect: 5
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 7

Resources
Expression Summary
histogram
Resources
Length (a.a.) 667
Molecular Weight (Da) 75,339
Isoelectric Point (pI) 5.64
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:483367 to 481364 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
This feature contains embedded feature(s): YBR121C-A
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 2011-02-03
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2004 483367..481364 2011-02-03 2011-02-03
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000325
SUMMARY PARAGRAPH for GRS1

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 (4, 5 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 (4, 5, 6 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for GRS1
1) Magrath C and Hyman LE  (1999) A mutation in GRS1, a glycyl-tRNA synthetase, affects 3'-end formation in Saccharomyces cerevisiae. Genetics 152(1):129-41
2) 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
3) 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
4) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
5) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
6) 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