PMID: 6159923Oct 17, 1980Paper

Protein synthesis defects in temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins

Biochimica Et Biophysica Acta
W S Champney

Abstract

The ribosomes from four temperature-sensitive mutants of Escherichia coli have been examined for defects in cell-free protein synthesis. The mutants examined had alterations in ribosomal proteins S10, S15, or L22 (two strains). Ribosomes from each mutant showed a reduced activity in the translation of phage MS2 RNA at 44 degrees C and were more rapidly inactivated by heating at this temperature compared to control ribosomes. Ribosomal subunits from three of the mutants demonstrated a partial or complete inability to reassociate at 44 degrees C. 70-S ribosomes from two strains showed a reducton in messenger RNA binding. tRNA binding to the 30 S subunit was reduced in the strains with altered 30-S proteins and binding to the 50 S subunit was affected in the mutants with a change in 50 S protein L22. The relation between ribosomal protein structure and function in protein synthesis in these mutants is discussed.

References

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Citations

Jul 1, 1992·The International Journal of Biochemistry·W S ChampneyR Samuels
Sep 13, 2002·Journal of Molecular Biology·Natalia DavydovaMaria Garber
Aug 15, 1989·Analytical Biochemistry·W S Champney
Oct 30, 2012·Cell·Krishna KannanAlexander S Mankin
Feb 20, 1985·Biochimica Et Biophysica Acta·J Armstrong-Major, W S Champney
Oct 1, 1994·Journal of Bacteriology·H S Chittum, W S Champney

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