GUS1/YGL245W Summary Help

Standard Name GUS1
Systematic Name YGL245W
Alias GSN1
Feature Type ORF, Verified
Description Glutamyl-tRNA synthetase (GluRS); forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm; protein abundance increases in response to DNA replication stress (1, 2, 3 and see Summary Paragraph)
Name Description GlUtamyl-tRNA Synthetase
Gene Product Alias GluRS
Chromosomal Location
ChrVII:39023 to 41149 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All GUS1 GO evidence and references
  View Computational GO annotations for GUS1
Molecular Function
Manually curated
High-throughput
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 9 genes
Resources
Large-scale survey
conditional
null
overexpression
reduction of function
Resources
139 total interaction(s) for 113 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 73
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 2
  • Biochemical Activity: 22
  • Co-crystal Structure: 1
  • PCA: 3
  • Protein-peptide: 3
  • Protein-RNA: 2
  • Reconstituted Complex: 6
  • Two-hybrid: 1

Genetic Interactions
  • Negative Genetic: 9
  • Positive Genetic: 10
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 708
Molecular Weight (Da) 80,842
Isoelectric Point (pI) 7.55
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:39023 to 41149 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2003-09-22 | Sequence: 2003-09-22
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2127 39023..41149 2003-09-22 2003-09-22
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 SGDIDS000003214
SUMMARY PARAGRAPH for GUS1

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 GUS1
1) Galani K, et al.  (2001) The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p. EMBO J 20(23):6889-98
2) Deinert K, et al.  (2001) Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem 276(8):6000-8
3) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
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