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Nucleic Acids Research, 1984, Vol. 12, No. 10 4377-4384
© 1984

ENZYMOLOGY

The ß subunit of E. coil glycyl-tRNA synthetase plays a major role in tRNA recognition

Glenn M. Nagel, Susan Cumberledge, Mark S. Johnson, Ezio Petrella and Bruce H. Weber

Department of Chemistry and Institute for Molecular Biology, California State University Fullerton, CA 92634, USA

Received February 2, 1984. Revised April 16, 1984. Accepted April 16, 1984.

The contributions made by the {alpha} and ß subunits of E. coli glycyl-tRNA synthetase to the recognition of tRNA have been investigated via binding and immunological methods. Using the nitrocellulose filter assay, we have shown that isolated ß subunit, but not the {alpha} subunit, binds [14C] glycyl-tRNA with an affinity comparable to that of the native enzyme. Further, the data indicate that the 6 subunit possesses one binding site for glycyl-tRNA while the native or reconstituted enzyme ({alpha}2ß2) has two sites. Rabbit antibodies directed at the ß subunit or the holoenzyme inhibit efficiently the ability of the enzyme to aminoacylate tRNA while {alpha}-subunit antibodies have a smaller effect. Since none of the antisera have an appreciable effect on the ATP-PPi exchange activity of the enzyme under these conditions, the ß-subunit (and holoenzyme) antisera evidently interfere with productive tRNA binding. Taken together, the data indicate that the larger, ß subunit of glycyl-tRNA synthetase plays a major role in tRNA recognition.


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