FRS2/YFL022C Summary Help

FRS2 BASIC INFORMATION

Standard Name FRS2
Systematic Name YFL022C
Feature Type ORF, Verified
Description Alpha subunit of cytoplasmic phenylalanyl-tRNA synthetase, forms a tetramer with Frs1p to form active enzyme; evolutionarily distant from mitochondrial phenylalanyl-tRNA synthetase based on protein sequence, but substrate binding is similar (1, 2 and see Summary Paragraph)
Name Description phenylalanyl (F)-tRNA Synthetase
Gene Product Alias cytoplasmic phenylalanyl-tRNA synthetase alpha subunit 1
GO Annotations All FRS2 GO evidence and references
    View Computational GO annotations for FRS2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All FRS2 Phenotype details and references
Large-scale survey
conditional
null
overexpression
Interactions FRS2 All interactions details and references
16 total interaction(s) for 12 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 1
  • Two-hybrid: 2
Sequence Information
ChrVI:95008 to 93497 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1512 95008..93497 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001872

FRS2 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for FRS2

SUMMARY PARAGRAPH for FRS2

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 FRS2]

1) Sanni A, et al.  (1988) Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase. J Biol Chem 263(30):15407-15
2) Aphasizhev R, et al.  (1996) Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site. Biochemistry 35(1):117-23
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