Literature DB >> 3122848

On the nature of antibiotic binding sites in ribosomes.

E Cundliffe1.   

Abstract

The ribosome is an enzyme and enzymes have active sites. Antibiotics that affect ribosomal function can be considered as enzyme inhibitors (or regulators) and it is therefore pertinent to identify their molecular targets as a means of studying the active sites of the particle. The methods available for doing this are considered and, in general terms, the data are evaluated. The conclusion is reached that there exists virtually no compelling evidence that antibiotics bind primarily to ribosomal proteins. Rather, studies of antibiotic resistance in various systems strongly suggest that ribosomal RNA is the primary target for a number of drugs. Moreover, in at least one case (relating to the antibiotic thiostrepton), such an effect can be demonstrated directly. These conclusions imply a fundamental role for RNA in ribosomal function.

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Year:  1987        PMID: 3122848     DOI: 10.1016/0300-9084(87)90213-6

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  26 in total

1.  Deleterious mutations in small subunit ribosomal RNA identify functional sites and potential targets for antibiotics.

Authors:  Aymen Yassin; Kurt Fredrick; Alexander S Mankin
Journal:  Proc Natl Acad Sci U S A       Date:  2005-11-03       Impact factor: 11.205

2.  Functional conformations of the L11-ribosomal RNA complex revealed by correlative analysis of cryo-EM and molecular dynamics simulations.

Authors:  Wen Li; Jayati Sengupta; Bimal K Rath; Joachim Frank
Journal:  RNA       Date:  2006-05-08       Impact factor: 4.942

3.  Mutations in the 915 region of Escherichia coli 16S ribosomal RNA reduce the binding of streptomycin to the ribosome.

Authors:  D Leclerc; P Melançon; L Brakier-Gingras
Journal:  Nucleic Acids Res       Date:  1991-07-25       Impact factor: 16.971

4.  The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt) binary and L11-rRNA(58 nt)-thiostrepton ternary complexes.

Authors:  Donghan Lee; Joseph D Walsh; Ping Yu; Michelle A Markus; Theodora Choli-Papadopoulou; Charles D Schwieters; Susan Krueger; David E Draper; Yun-Xing Wang
Journal:  J Mol Biol       Date:  2007-01-10       Impact factor: 5.469

5.  50S ribosomal subunit synthesis and translation are equivalent targets for erythromycin inhibition in Staphylococcus aureus.

Authors:  W S Champney; R Burdine
Journal:  Antimicrob Agents Chemother       Date:  1996-05       Impact factor: 5.191

6.  Mechanism of action of streptogramins and macrolides.

Authors:  P Vannuffel; C Cocito
Journal:  Drugs       Date:  1996       Impact factor: 9.546

7.  Mapping posttranscriptional modifications in 5S ribosomal RNA by MALDI mass spectrometry.

Authors:  F Kirpekar; S Douthwaite; P Roepstorff
Journal:  RNA       Date:  2000-02       Impact factor: 4.942

8.  Yeast glycosylation mutants are sensitive to aminoglycosides.

Authors:  N Dean
Journal:  Proc Natl Acad Sci U S A       Date:  1995-02-28       Impact factor: 11.205

Review 9.  Targeting RNA in mammalian systems with small molecules.

Authors:  Anita Donlic; Amanda E Hargrove
Journal:  Wiley Interdiscip Rev RNA       Date:  2018-05-03       Impact factor: 9.957

10.  Methylation of 23S rRNA caused by tlrA (ermSF), a tylosin resistance determinant from Streptomyces fradiae.

Authors:  M Zalacain; E Cundliffe
Journal:  J Bacteriol       Date:  1989-08       Impact factor: 3.490

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