Protein folding in Escherichia coli: role of 23S ribosomal RNA

• Published in: Biochimica et biophysica acta Vol. 1429; no. 2; pp. 293 - 298
• Main Authors: Chattopadhyay, Subrata, Pal, Saumen, Pal, Debashis, Sarkar, Dibyendu, Chandra, Suparna, Das Gupta, Chanchal
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 11.01.1999
• Subjects: Aminoglycosides; Anti-Bacterial Agents - pharmacology; beta-Galactosidase - biosynthesis; beta-Galactosidase - chemistry; Chloramphenicol; Chloramphenicol - pharmacology; Escherichia coli - metabolism; Lincomycin; Lincomycin - pharmacology; Protein Folding; Protein Synthesis Inhibitors - pharmacology; Ribosomal RNA; RNA, Ribosomal, 23S - metabolism; Streptomycin - pharmacology; Chloramphenicol; Lincomycin; Protein folding; Ribosomal RNA
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/S0167-4838(98)00179-4

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 β-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 β-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.