Literature DB >> 6819001

Stabilization of the ternary complex EF-Tu.GTP.valyl-tRNAval by ammonium salts.

B Antonsson, R Leberman.   

Abstract

In a search for crystallizing conditions for the ternary complex EF-Tu.GTP.valyl-tRNAval, the influence of various salts on its stability has been examined by measuring the rate of deacylation of the aminoacyl-tRNA in the complex. The most striking result is the general higher stability in solutions of ammonium salts and, in particular, the enhancement of this effect by sulphate and citrate. Thus sodium sulphate and citrate lead to destabilization of the complex, as expected from conventional considerations of adding salt, whereas the corresponding ammonium salts stabilize the complex as shown, for example, by an increase in the half-life of the valyl-tRNAval in the complex from about 20 hours to at least 300 hours in the presence of 1.2 M ammonium sulphate. These results suggest that ammonium sulphate and ammonium citrate might be very suitable precipitants for crystallization studies of the ternary complex.

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Year:  1982        PMID: 6819001     DOI: 10.1016/s0300-9084(82)80384-2

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


  3 in total

1.  Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.

Authors:  Lee E Sanderson; Olke C Uhlenbeck
Journal:  J Mol Biol       Date:  2007-02-06       Impact factor: 5.469

2.  Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA.

Authors:  J P Abrahams; B Kraal; B F Clark; L Bosch
Journal:  Nucleic Acids Res       Date:  1991-02-11       Impact factor: 16.971

3.  Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome.

Authors:  Darius Kavaliauskas; Chunlai Chen; Wei Liu; Barry S Cooperman; Yale E Goldman; Charlotte R Knudsen
Journal:  Nucleic Acids Res       Date:  2018-09-19       Impact factor: 16.971

  3 in total

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