Covalent attachment of fluorescent probes to the X-base of Escherichia coli phenylalanine transfer ribonucleic acid
Open Access
- 1 January 1977
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 4 (7) , 2161-2168
- https://doi.org/10.1093/nar/4.7.2161
Abstract
Was labeled with the N-hydroxysuccinimide esters of 1-dimethylaminaphthalene-5-sulfonyl glycine and N-methylanthranilic acid through reaction with the amino acid moiety of its X-base, whereby yields of 66% and 24%, respectively, were obtained. The purified dimethylaminonaphthalene-sulfonate derivative could not be aminoacylated and was found to a strong competitive inhibitor of phenyialanine-tRNA synthetase [Ki=8×10−7 M]. The N-methylanthraniloyl could be charged to an exten of 5% as compared to native tRNAPhe. The fluorescence emission spectra of the derivatives are indicative of a slightly hydrophobic environment for both fluorophores. The results suggest that the integrity of the polar amino acid group of the X-base is required for the maintenance of the biologically active conformation.Keywords
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