Protein folding in Escherichia coli: role of 23S ribosomal RNA.
Post-translational control of Escherichia coli ribosome on newly synthesised polypeptide leading to its active conformation (protein folding) has been shown in the case of the enzyme beta-galactosidase. As expected, antibiotics chloramphenicol and lincomycin, which bind to 23S rRNA/50S subunit and kasugamycin and streptomycin which interact with the 30S subunit instantaneously inhibited protein synthesis when they were added to the growing cells. The increase in beta-galactosidase activity, though stopped immediately after the addition of chloramphenicol and lincomycin, went on considerably in the presence of streptomycin and kasugamycin even after the stoppage of protein synthesis.
Chattopadhyay
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S
Department of Biophysics, Molecular Biology and Genetics, University College of Science, Calcutta, India.
Pal
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S
Pal
D
D
Sarkar
D
D
Chandra
S
S
Das Gupta
C
C
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002701:Chloramphenicol / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D008034:Lincomycin / Q000494:pharmacology; D017510:Protein Folding; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D012338:RNA, Ribosomal, 23S / Q000378:metabolism*; D013307:Streptomycin / Q000494:pharmacology; D001616:beta-Galactosidase / Q000096:biosynthesis / Q000737:chemistry