NDLI: Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID

Content Provider	Journal of Biological Chemistry (JBC)
Author	Lapointe, Jacques Söll, Dieter
Abstract	Escherichia coli glutamyl transfer ribonucleic acid synthetase acylates the three homologous tRNAglu isoacceptors with very similar Km values (2.4 to 4.6 x 10-7 m). The pure enzyme forms a 1:1 complex with its cognate tRNA as judged by gradient centrifugation and fluorescence-quenching studies. The biological specificity of complex formation is not strictly observed in vitro since fluorescence-quenching studies demonstrate complexes of this enzyme with Escherichia coli tRNAval and tRNAleu. Studies on the protection by tRNAglu against heat inactivation of the enzyme give a binding constant of 3.6 x 10-7 m for this interaction. Experiments performed in this paper indicate a concerted mechanism of glutamyl-tRNA formation.
Related Links	http://www.jbc.org/content/247/16/4975.abstract
Ending Page	4981
Starting Page	4975
Page Count	7
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	16
Volume Number	247
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1972-08-25
Access Restriction	Open
Alternative Title	Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID