Difference between revisions of "YLL018C"

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'''Description of YLL018C:''' 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<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000056730'>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 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000062732'>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 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062744'>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 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
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'''Description of YLL018C:''' 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<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 {{SGDpaper|S000076273}} PMID 12888345</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062732'>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 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000056730'>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 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062744'>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
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{{SGDpaper|S000062744}} PMID 10873455</ref>
 
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Revision as of 14:05, 25 February 2010

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Systematic name YLL018C
Gene name DPS1
Aliases
Feature type ORF, Verified
Coordinates Chr XII:111574..109901
Primary SGDID S000003941


Description of YLL018C: 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]




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References

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  1. Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 SGD PMID 8450889
  2. Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 SGD PMID 12888345
  3. Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 SGD PMID 3297688
  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 SGD PMID 3286258
  5. Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 SGD PMID 2047878
  6. 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 SGD PMID 2047877
  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 SGD PMID 10873455

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