Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase

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Abstract
Gene deletions show that much of Escherichia coli alanine tRNA synthetase is dispensable for each of 3 activities and that these activities appear to require specific domains arranged linearly along the polypeptide. Thus, variable fusions of extra polypeptide domains to a catalytic core may account for the diverse sizes of aminoacyl tRNA synthetases.