GRS1/YBR121C Summary Help

GRS1 BASIC INFORMATION

Standard Name GRS1
Systematic Name YBR121C
Feature Type ORF, Verified
Description Cytoplasmic and mitochondrial glycyl-tRNA synthase that 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 (1, 2 and see Summary Paragraph)
Name Description Glycyl-tRNA Synthase 2
Gene Product Alias glycyl-tRNA synthetase 2
GO 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
Mutant Phenotype All GRS1 Phenotype details and references
Classical genetics
reduction of function
Large-scale survey
conditional
null
overexpression
Interactions GRS1 All interactions details and references
25 total interaction(s) for 22 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Biochemical Activity: 1

Genetic Interactions
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 1
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 8

Sequence Information
ChrII:483361 to 481358 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
This feature contains embedded feature(s): YBR121C-A
Gbrowse
Last Update Coordinates: 2004-07-16 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2004 483361..481358 2004-07-16 1997-01-28
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000325

GRS1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

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Expression Summary histogram

SUMMARY PARAGRAPH for GRS1

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).

Last updated: 2008-07-14

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GRS1]

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) 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
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