Other names published for DPS1: aspartyl-tRNA synthetase, AspRS, aspartate--tRNA ligase DPS1, YLL018C
DPS1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
DPS1 - Function/Process (32)
| Reference | Other Genes Addressed |
|---|---|
| Ador L, et al. (2004) Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase. Biochemistry 43(22):7028-37 | |
| Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 | |
| Walter F, et al. (2002) Binding of tobramycin leads to conformational changes in yeast tRNA(Asp) and inhibition of aminoacylation. EMBO J 21(4):760-8 | |
| Moulinier L, et al. (2001) The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. EMBO J 20(18):5290-301 | |
| Frugier M, et al. (2000) A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding. EMBO J 19(10):2371-80 | |
| 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 | |
| Ador L, et al. (1999) Active site mapping of yeast aspartyl-tRNA synthetase by in vivo selection of enzyme mutations lethal for cell growth. J Mol Biol 288(2):231-42 | |
| Eriani G and Gangloff J (1999) Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs. J Mol Biol 291(4):761-73 | |
| Sauter C, et al. (1999) Crystallogenesis studies on yeast aspartyl-tRNA synthetase: use of phase diagram to improve crystal quality. Acta Crystallogr D Biol Crystallogr 55(Pt 1):149-56 | |
| Schimmel P and Wang CC (1999) Getting tRNA synthetases into the nucleus. Trends Biochem Sci 24(4):127-8 | |
| Wolfson AD, et al. (1999) Mimics of yeast tRNAAsp and their recognition by aspartyl-tRNA synthetase. Biochemistry 38(37):11926-32 | |
| Sissler M, et al. (1997) Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase. Nucleic Acids Res 25(24):4899-906 | |
| Eriani G, et al. (1995) The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site. J Mol Evol 40(5):499-508 | |
| Frugier M, et al. (1994) Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 33(33):9912-21 | |
| Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 | |
| Eriani G, et al. (1993) Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline. Proc Natl Acad Sci U S A 90(22):10816-20 | |
| Martin F, et al. (1993) Overproduction and purification of native and queuine-lacking Escherichia coli tRNA(Asp). Role of the wobble base in tRNA(Asp) acylation. J Mol Biol 234(4):965-74 | |
| Puglisi JD, et al. (1993) Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase. Nucleic Acids Res 21(1):41-9 | |
| Eriani G, et al. (1991) Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organisation by deletion analysis. Eur J Biochem 200(2):337-43 | |
| Gasparini S, et al. (1991) Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Biochemistry 30(17):4284-9 | |
| Kern D, et al. (1990) The three cysteine residues of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae are not essential for its activity. Eur J Biochem 193(1):97-103 | |
| Gampel A and Tzagoloff A (1989) Homology of aspartyl- and lysyl-tRNA synthetases. Proc Natl Acad Sci U S A 86(16):6023-7 | |
| Prevost G, et al. (1989) Study of the arrangement of the functional domains along the yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 180(2):351-8 | |
| 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 | |
| Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 | |
| Mejdoub H, et al. (1987) Covalent aspartylation of aspartyl-tRNA synthetase from bakers' yeast by its cognate aspartyl adenylate: identification of the labeled residues. Biochemistry 26(7):2054-9 | |
| Podjarny A, et al. (1987) Yeast tRNA(Asp)-aspartyl-tRNA synthetase complex: low resolution crystal structure. J Biomol Struct Dyn 5(2):187-98 | |
| Sellami M, et al. (1985) Isolation and characterization of the yeast aspartyl-tRNA synthetase gene. Gene 40(2-3):349-52 | |
| Hounwanou N, et al. (1983) Primary structure of aspartyl-tRNA synthetase from baker's yeast: tryptic and CNBr peptides. Biochimie 65(7):379-88 | |
| Moras D, et al. (1983) Yeast tRNAAsp-aspartyl-tRNA synthetase: the crystalline complex. J Biomol Struct Dyn 1(1):209-23 | |



