MES1/YGR264C Summary Help

Standard Name MES1
Systematic Name YGR264C
Feature Type ORF, Verified
Description Methionyl-tRNA synthetase; forms a complex with glutamyl-tRNA synthetase (Gus1p) and Arc1p, which increases the catalytic efficiency of both tRNA synthetases; also has a role in nuclear export of tRNAs (1, 2, 3, 4 and see Summary Paragraph)
Also known as: MESI
Name Description MEthionyl-tRNA Synthetase
Gene Product Alias MetRS 5 , methionyl-tRNA synthetase 1
Chromosomal Location
ChrVII:1021853 to 1019598 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 204 cM
Gene Ontology Annotations All MES1 GO evidence and references
  View Computational GO annotations for MES1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 10 genes
Resources
Classical genetics
conditional
Large-scale survey
conditional
null
reduction of function
unspecified
Resources
60 total interaction(s) for 37 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 31
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 2
  • Biochemical Activity: 1
  • Co-crystal Structure: 1
  • Protein-peptide: 1
  • Reconstituted Complex: 5

Genetic Interactions
  • Negative Genetic: 8
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 4
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 751
Molecular Weight (Da) 85,677
Isoelectric Point (pI) 6.59
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:1021853 to 1019598 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 204 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2256 1021853..1019598 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 SGDIDS000003496
SUMMARY PARAGRAPH for MES1

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 (6, 7 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 (6, 7, 8 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for MES1
1) Chatton B, et al.  (1987) Cloning and characterization of the yeast methionyl-tRNA synthetase mutation mes1. J Biol Chem 262(31):15094-7
2) 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
3) Feng W and Hopper AK  (2002) A Los1p-independent pathway for nuclear export of intronless tRNAs in Saccharomycescerevisiae. Proc Natl Acad Sci U S A 99(8):5412-7
4) 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
5) Simos G, et al.  (1996) The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J 15(19):5437-48
6) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
7) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
8) 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