Open AccessThe Effect of Chemical Modification of the CCA End of Yeast tRNA Phe on Its Biological Activity on Ribosomes
Author(s) -
KRUSE Torben A.,
SIBOSKA Gunhild E.,
SPRINZL Mathias,
CLARK Brian F. C.
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04616.x
Subject(s) - transfer rna , ribosome , alkylation , residue (chemistry) , yeast , chemistry , peptide , biochemistry , stereochemistry , escherichia coli , rna , catalysis , gene
Yeast tRNA Phe containing 2‐thiocytidine (s 2 C) at position 75 was alkylated specifically at this residue. The biological activities of alkylated and native tRNA Phe were compared in an Escherichia coli protein‐synthesizing system in vitro. The alkylated tRNA Phe proved to be active in all steps involved in the elongation phase but the rate of the peptide transfer reaction was somewhat lower when the alkylated tRNA Phe acted as an acceptor of peptidyl residues as compared to native tRNA Phe . These results raise the possibility for attaching spectroscopic or affinity labels at the s 2 C‐75 residue of tRNA Phe without impairing the activity of the tRNA.