Literature DB >> 3902099

The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae.

I Amiri, H Mejdoub, N Hounwanou, Y Boulanger, J Reinbolt.   

Abstract

The crystallizable cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae is a dimer made up of identical subunits (Mr 63 000). Its primary structure was established using peptide sequences from four different digests of the native and citraconylated enzyme with trypsin, cyanogen bromide and staphylococcal protease. The oligonucleotide sequence of the structural gene was used as a template for the final alignment of the various peptides in the correct order.

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Year:  1985        PMID: 3902099     DOI: 10.1016/s0300-9084(85)80200-5

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  2 in total

1.  Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA.

Authors:  M Sellami; F Fasiolo; G Dirheimer; J P Ebel; J Gangloff
Journal:  Nucleic Acids Res       Date:  1986-02-25       Impact factor: 16.971

2.  Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.

Authors:  G Eriani; J Cavarelli; F Martin; G Dirheimer; D Moras; J Gangloff
Journal:  Proc Natl Acad Sci U S A       Date:  1993-11-15       Impact factor: 11.205

  2 in total

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