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J Bacteriol. 1974 February; 117(2): 351-359
Copyright © 1974 American Society for Microbiology. All Rights Reserved.
1 Department of Biological Chemistry, The Pennsylvania State University, Hershey Medical Center, Hershey, Pennsylvania 17033
ABSTRACT
The Escherichia coli suppressor mutation, supT, has been shown to cause a C
U substitution in the middle position of the tRNAGGGGly anticodon. This is the same tRNA species that is altered by the glyUsuAGA mutation studied previously. This finding indicates that the supT mutant tRNA reads the glutamic acid codon, GAG. The supT suppressor has also been converted to a new suppressor, called glyUsuGAA, which will suppress the GAA mutation, trpA46. The in vivo suppression efficiencies of each of these three missense suppressors has been measured and are as follows: glyUsuAGA, 3.6%; supT, 1.6%; and glyUsuGAA, 0.4%. Mistranslation by these mutant glycine tRNA species has no adverse affects on cell growth since cultures possessing the suppressors grow as fast as cells without. The supT tRNA species can be observed as a peak in the profile of glycyl-tRNA fractionated on a RPC-5 chromatographic column, indicating that the mutant tRNA can be aminoacylated with reasonable efficiency. This finding contrasts with previous findings concerning the glyUsuAGA mutant tRNA which is not significantly aminoacylated under the same conditions.
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