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Start Over Author "Sever, Sanja" Journal biochemistry
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1. Escherichia coli tryptophanyl mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding

Author

Sever, Sanja, Rogers, Kelly, Rogers, M. John, Carter, Charles, Jr., and Soll, Dieter

Subjects
Aminoacyl-tRNA synthetases -- Analysis, Proteins -- Synthesis, Biological sciences, Chemistry
Abstract

Tryptophanyl-tRNA synthetases (TrpRS) isolated from six auxotrophic strains of Escherichia coli with mutations in the genes encoding TrpRS were examined for changes in aminoacylation and amino acid activation during protein synthesis. The results show that in the tryptophan/tyrosine subclass of class I aminoacyl tRNA synthetases, dimerization ensures the proper configuration of the enzyme active sites for proper enzyme recognition of its cognate amino acids during protein synthesis.

Published
1996

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