Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site.
Recent data suggest that size polymorphism of aminoacyl tRNA synthetase is due to variable fusions of additional functional domains to a catalytic core so that, in a large synthetase, a substantial part of the polypeptide is dispensable for catalytic activity. We demonstrate here that a dispensable domain, joined to the catalytic core of a large synthetase, can activate the catalytic sites. This is shown by complementation of an activity-deficient mutant enzyme by protein fragments that contain internal deletions within the catalytic domain and are themselves devoid of activity. The complementation is dependent upon the presence of a defined segment of polypeptide that is remote in the sequence from the catalytic core. Substantial coupling has been established between dispensable and indispensable component pieces. This could be a mechanism to build efficiently large enzymes which integrate the catalytic sites with other previously shown functional roles.
D000412:Alanine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics*; D001665:Binding Sites; D002872:Chromosome Deletion; D000939:Epitopes / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005816:Genetic Complementation Test; D007074:Immunoglobulin G; D010957:Plasmids
D000939:Epitopes; D007074:Immunoglobulin G; D000604:Amino Acyl-tRNA Synthetases; D000412:Alanine-tRNA Ligase