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Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2

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Summary

During protein synthesis the interaction with ribosomes of elongation factors Tu (EF-Tu), G (EF-G) and initiation factor 2 (IF-2) is associated with the hydrolysis of GTP which is directly related to the functions of the factors. In this article we review systematically the properties of these GTPase activities in the presence and absence of protein synthesis, and by examining the characteristics of the different minimal systems for the expression of these activities we point to the role of the various effectors and to the enzymological aspects of the systems. For EF-Tu, it has been possible to eliminate any requirement for macromolecular effectors, showing that the factor itself is a GTPase. For EF-G, the presence of at least the 50S ribosomal subunit has remained a requirement, whereas IF-2 needs both the 50S and 30S subunits to exibit GTPase activity. Between the GTPase activities of the three factors there are some striking similarities, but important differences prevail as a consequence of the specificity of the different functions. This can also be seen by examining the respective ribosomal regions implicated in these reactions. When coupled with protein synthesis, the three GTPase activities reveal characteristics differing from those observed in partial systems.

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Abbreviations

EF-Tu:

elongation factor Tu

EF-Ts:

elongation factor Ts

EF-T:

EF-Tu·EF-Ts

EF-G:

elongation factor G

IF-2:

initiation factor 2

GTPase:

guanosine 5′-triphosphatase (EC 3.6.1.-)

tNRAPhe :

purified phenylalanine-accepting transfer ribonucleic acid

A site:

ribosomal site binding aa-tRNA out of the ternary complex EF-Tu

GTP:

aa-tRNA

P site:

ribosomal site binding peptidyl-tRNA prior to peptide bond formation

aa-tRNA:

aminoacyl-tRNA

mRNA:

messenger RNA

poly(U):

poly(uridylic) acid

M+ :

monovalent cation

SDS:

sodium dodecyl sulfate

GTP:

guanosine 5′-triphosphate

GDP:

guanosine 5′-diphosphate

GMPPCP:

guanylyl methylene diphosphonate

GMPPNP:

guanylyl imino diphosphate

EDTA:

ethylene diamine tetra-acetic acid

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  1. Gernot Sander

    Present address: Max-Planck-Institut für Molekulare Genetik, Ihnestr. 63-73, 1000, Berlin 33, Federal Republic of Germany

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  1. Laboratoire de Biochimie, Ecole Polytechnique, Laboratoire associé no 240 du Centre National de la Recherche Scientifique, 91128, Palaiseau Cedex, France

    Andrea Parmeggiani &  Gernot Sander

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  1. Andrea Parmeggiani
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Parmeggiani, A., Sander, G. Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2. Mol Cell Biochem 35, 129–158 (1981). https://doi.org/10.1007/BF02357085

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