Modular arrangement of functional domains along the sequence of an aminoacyl transfer rna synthetase
Jasin, M.; Regan, L.; Schimmel, P.
Nature (London) 306(5942): 441-447
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.