ALTHOUGH the basic mechanisms of protein synthesis are now rather well understood, particularly in Escherichia coli, it is less clear how the high accuracy of this process is achieved. (The error rate in protein synthesis in E. coli seems to be about one in 104 amino acid misincorporations (Edelman and Gallant, unpublished results, and our own unpublished data)). A major site determining accuracy in protein synthesis is the ribosome, and in addition to the ribosome-mediated effects on accuracy (in vivo and in vitro) of various metal ions, aminoglycoside antibiotics and organic solvents, there are ribosomal mutations which increase or decrease accuracy2. Certain mutations of the 30S ribosomal protein SI2 conferring streptomycin resistance (the strA locus) enhance accuracy3–5, whereas certain mutations in the S4 protein (the ram locus) are known to decrease accuracy6. The strA mutations are restrictive (reducing) in their effect on both missense and nonsense suppression in vivo and on miscoding in vitro3, the ram mutation, on the other hand, has the opposite effect in both cases6. It is possible that it is the kinetics of polypeptide synthesis at the ribosome that determines accuracy and that the kinetics in turn are affected by the strA and ram mutations. Because the same transfer RNA (tRNA) discrimination kinetics that may determine accuracy may also contribute to the elongation speed, we have investigated the effect of mutation to streptomycin resistance on the speed of polypeptide elongation.
Access optionsAccess options
Subscribe to Journal
Get full journal access for 1 year
only $3.90 per issue
All prices are NET prices.
VAT will be added later in the checkout.
Rent or Buy article
Get time limited or full article access on ReadCube.
All prices are NET prices.
Loftfield, R. B., Biochem. J., 89, 82–92 (1963).
Gorini, L., and Davies, J., Curr. Top. Microbiol. Immun., 44, 100–122 (1968).
Gorini, L., and Kataja, E., Proc. natn. Acad. Sci. U.S.A., 51, 487 (1964).
Gorini, L., Cold Spring Harb. Symp. quant. Biol., 31, 101–111 (1969).
Gorini, L., Nature new Biol., 234, 261–264 (1972).
Rosset, R., and Gorini, L., J. molec. Biol., 39, 95–112 (1969).
Ninio, J., J. molec. Biol., 84, 297–313 (1974).
Kepes, A., and Bequin, S., Biochim. biophys. Acta, 123, 546–560. (1966).
Lacroute, F., and Stent, G. S., J. molec. Biol., 35, 165–173 (1968).
Kepes, A., Biochim. biophys. Acta. 76, 293–309 (1963).
Ozaki, M., Mizushima, S., Nomura, M., Nature, 222, 333–339 (1969).
Leive, L., Biochem. biophys. Res. Commun., 20, 321–327 (1965).
Perlman, R., and Pastan, I., Biochem. biophys. Res. Commun., 30, 656–664 (1968).
Gupta, R., and Schlessinger, D., J. Bact., 125, 84–93 (1976).
Zabin, I., and Fowler, A. V., in The Lactose Operon (edit. by Beckwith, J. R., and Zipser, D.) (Cold Spring Harbor Laboratory, New York, 1970).
About this article
Antimicrobial drug resistance affects broad changes in metabolomic phenotype in addition to secondary metabolism
Proceedings of the National Academy of Sciences (2013)
Trends in Biochemical Sciences (2001)
Suppression of rpsL phenotypes by tuf mutations reveals a unique relationship between translation elongation and growth rate
Molecular Microbiology (1993)
Mutant sequences in the rpsL gene of Escherichia coli B/r: Mechanistic implications for spontaneous and ultraviolet light mutagenesis
MGG Molecular & General Genetics (1992)
MGG Molecular & General Genetics (1987)