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Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain


Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain



European Journal of Biochemistry 174(1): 155-161



ISSN/ISBN: 0014-2956

PMID: 3286258

DOI: 10.1111/j.1432-1033.1988.tb14076.x

Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae is a dimer made up of identical subunits of Mr 64,000 as shown by biochemical and crystallographic analyses. Previous studies have emphasized the high sensitivity of the amino-terminal region (residues 1-32) to proteolytic enzymes. This work reports the results of limited tryptic or chymotryptic digestion of the purified enzyme which gives rise to a truncated species that has lost the first 50-64 residues with full retention of both the activity and the dimeric structure. In contrast the larger tryptic fragment is distinguished from the whole enzyme by its weaker retention on heparin-substituted agarose gels. The cleaved N-terminal part presents peculiar structural features, such as a high content in lysine residues arranged in a palindromic fashion. The properties of the trypsin-modified enzyme and of the cleaved amino-terminal region are discussed in relation to the known structural characteristics of aspartyl-tRNA synthetase and of other eukaryotic aminoacyl-tRNA synthetases.

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Accession: 016791294

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