DPS1/YLL018C Summary Help

Standard Name DPS1 1
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; shares five highly conserved amino acids with human that when mutated cause leukoencephalopathy characterized by hypomyelination with brain stem and spinal cord involvement and leg spasticity (HBSL) (2, 3, 4, 5, 6, 7, 8, 9 and see Summary Paragraph)
Gene Product Alias AspRS 10 , aspartyl-tRNA synthetase 10
Chromosomal Location
ChrXII:111575 to 109902 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology 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
Regulators 9 genes
Resources
Classical genetics
null
Large-scale survey
null
overexpression
repressible
unspecified
Resources
61 total interaction(s) for 55 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 22
  • Co-purification: 1
  • Protein-peptide: 2
  • Reconstituted Complex: 2
  • Two-hybrid: 3

Genetic Interactions
  • Negative Genetic: 9
  • Positive Genetic: 1
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 557
Molecular Weight (Da) 63,515
Isoelectric Point (pI) 6.54
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXII:111575 to 109902 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1674 111575..109902 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 SGDIDS000003941
SUMMARY PARAGRAPH for DPS1

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 (11, 12 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 (11, 12, 13 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for DPS1
1) Purnelle B and Goffeau A  (1997) The sequence of 32b on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABS transporter homologous to the human multidrug resistance protein. Yeast 13(2):183-8
2) Cavarelli J, et al.  (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
3) 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
4) Putz J, et al.  (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9
5) 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
6) Lorber B, et al.  (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17
7) 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
8) Frugier M and Giege R  (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
9) Taft RJ, et al.  (2013) Mutations in DARS Cause Hypomyelination with Brain Stem and Spinal Cord Involvement and Leg Spasticity. Am J Hum Genet 92(5):774-80
10) Sellami M, et al.  (1985) Isolation and characterization of the yeast aspartyl-tRNA synthetase gene. Gene 40(2-3):349-52
11) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
12) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
13) 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