DPS1/YLL018C Summary Help

DPS1 BASIC INFORMATION

Standard Name DPS1
Systematic Name YLL018C
Feature Type ORF, Verified
Description Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation (1, 2, 3, 4, 5, 6, 7 and see Summary Paragraph)
Gene Product Alias AspRS 8 , aspartyl-tRNA synthetase 8
GO Annotations All DPS1 GO evidence and references
    View Computational GO annotations for DPS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All DPS1 Phenotype details and references
Large-scale survey
null
repressible
Interactions DPS1 All interactions details and references
49 total interaction(s) for 48 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 11
  • Biochemical Activity: 22
  • Two-hybrid: 2
Genetic Interactions
  • Phenotypic Enhancement: 9
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2
Sequence Information
ChrXII:111574 to 109901 | 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..1674 111574..109901 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000003941

DPS1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Localization Resources
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  • Functional Analysis

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Expression Summary histogram

ADDITIONAL INFORMATION for DPS1

SUMMARY PARAGRAPH for DPS1

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 (9, 10 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 (9, 10, 11 and references therein).

Last updated: 2008-07-14

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for DPS1]

1) Cavarelli J, et al.  (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
2) Ruff M, et al.  (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9
3) Putz J, et al.  (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9
4) Lorber B, et al.  (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61
5) Lorber B, et al.  (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17
6) Sauter C, et al.  (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24
7) Frugier M and Giege R  (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
8) Sellami M, et al.  (1985) Isolation and characterization of the yeast aspartyl-tRNA synthetase gene. Gene 40(2-3):349-52
9) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
10) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
11) 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