Journal
MOLECULAR MICROBIOLOGY
Volume 80, Issue 1, Pages 54-67Publisher
WILEY
DOI: 10.1111/j.1365-2958.2011.07555.x
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Funding
- Human Frontiers of Science Organization [RGY0088/2008]
- Estonian Science Foundation [8197, 7509]
- Estonian Ministry of Education and Research [SF0180166s08, SF0180164s08, SF0180026s09]
- Center of Excellence in Chemical Biology (Institute of Technology, University of Tartu)
- EU through Estonian Centre of Excellence in Genomics
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P>Inhibitors of protein synthesis cause defects in the assembly of ribosomal subunits. In response to treatment with the antibiotics erythromycin or chloramphenicol, precursors of both large and small ribosomal subunits accumulate. We have used a pulse-labelling approach to demonstrate that the accumulating subribosomal particles maturate into functional 70S ribosomes. The protein content of the precursor particles is heterogeneous and does not correspond with known assembly intermediates. Mass spectrometry indicates that production of ribosomal proteins in the presence of the antibiotics correlates with the amounts of the individual ribosomal proteins within the precursor particles. Thus, treatment of cells with chloramphenicol or erythromycin leads to an unbalanced synthesis of ribosomal proteins, providing the explanation for formation of assembly-defective particles. The operons for ribosomal proteins show a characteristic pattern of antibiotic inhibition where synthesis of the first proteins is inhibited weakly but gradually increases for the subsequent proteins in the operon. This phenomenon most likely reflects translational coupling and allows us to identify other putative coupled non-ribosomal operons in the Escherichia coli chromosome.
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