The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae |
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Authors: | I Amiri H Mejdoub N Hounwanou Y Boulanger J Reinbolt |
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Affiliation: | Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes 67084 Strasbourg Cedex (France) |
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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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Keywords: | aspartyl-tRNA synthétase structure primaire aspartyl-tRNA synthetase amino acid sequence |
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