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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Apr;87(7):2657–2661. doi: 10.1073/pnas.87.7.2657

Structure and probable genetic location of a "ribosome modulation factor" associated with 100S ribosomes in stationary-phase Escherichia coli cells.

A Wada 1, Y Yamazaki 1, N Fujita 1, A Ishihama 1
PMCID: PMC53749  PMID: 2181444

Abstract

The decrease in overall translation activity occurring concomitantly with the transition from the exponential growth phase to the stationary phase of Escherichia coli cells was found to be accompanied by the appearance of 100S ribosomes (dimers of 70S ribosome monomers). Analysis of ribosomal proteins by the radical-free and highly reducing method of two-dimensional gel electrophoresis indicated that a protein, designated protein E, was exclusively associated with 100S ribosomes. From the results, we propose that protein E is a "ribosome modulation factor" (RMF), which associates with 70S ribosomes and converts them to a dimeric form. A homology search of the partial amino acid sequence of RMF using the DNA sequence data bases revealed that the rmf gene, which encodes RMF, is located next to the fabA gene at 21.8 min on the E. coli chromosome.

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Selected References

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