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

Chattopadhyay, Subrata ; Pal, Saumen ; Pal, Debashis ; Sarkar, Dibyendu ; Chandra, Suparna ; Das Gupta, Chanchal (1999) Protein folding in Escherichia coli: role of 23S ribosomal RNA Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1429 (2). pp. 293-298. ISSN 0167-4838

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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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Protein Folding; Ribosomal RNA; Chloramphenicol; Lincomycin
ID Code:8869
Deposited On:28 Oct 2010 10:42
Last Modified:28 May 2011 09:18

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