Interaction of elongation factor 2 from wheat germ with guanosine nucleotides and ribosomes.

Abstract:

:1. The amino acid composition of wheat germ EF2 differs to some extent from that of elongation factors from mammals and bacteria. 2. The purified wheat germ EF2, similarly as the factors from other sources, is active in the: EF1-dependent polymerization of phenylalanine; ribosome-dependent GTP hydrolysis; binding of guanosine nucleotides; and ADP-ribosylation in the presence of diphtheria toxin. Fusidic acid at a concentration of 1 mM inhibits all these EF2-dependent reactions. 3. Diphtheria toxin in the presence of NAD+ inhibits polymerization of phenylalanine but does not effect GTP binding to EF2. 4. Binding of GDP to wheat germ EF2 is inhibited by ribosomes. During interaction with ribosomes, GTP in EF2-GTP complex is rapidly hydrolysed to GDP. Both GTP and 5'-guanylmethylenediphosphonate competitively inhibit formation of the ribosome-EF2-GDP complex due to the replacement of GDP from the complex. The latter is stabilized by fusidic acid.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Twardowski T,Legocki A

subject

Has Abstract

pub_date

1977-01-01 00:00:00

pages

21-33

issue

1

eissn

0001-527X

issn

1734-154X

journal_volume

24

pub_type

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