Open AccessAbout the specificity of photoinduced affinity labeling of Escherichia coli ribosomes by dihydrorosaramicin, a macrolide related to erythromycin
Author(s) -
SIEGRIST Sylvie,
MOREAU Nicole,
GOFFIC François
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09278.x
Subject(s) - puromycin , escherichia coli , ribosome , chromophore , effector , biochemistry , chemistry , binding site , biology , microbiology and biotechnology , protein biosynthesis , photochemistry , rna , gene
Photoactivation of the [ 3 H]dihydrorosaramicin chromophore at a wavelength above 300 nm allows the covalent attachment of the macrolide antibiotic to the bacterial ribosome. Bidimensional electrophoresis shows that the radioactivity is mainly associated with proteins L1, L5, L6, L15, L18, L19, S1, S3, S4, S5 and S9. When photoincorporation of the drug is conducted in the presence of puromycin as effector of [ 3 H]dihydrorosaramicin‐binding sites, a decrease in the labeling of most proteins is observed, except for L18 and L19, which are radiolabeled to a larger extent. These results allow us to speculate that L18 and L19 belong to the high‐affinity binding site of rosaramicin antibiotic.