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GTPases of the Translation Apparatus

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Abstract

Protein biosynthesis is a complex biochemical process involving a number of stages at which different translation factors specifically interact with ribosome. Some of these factors belong to GTP-binding proteins, or G-proteins. Due to their functioning, GTP is hydrolyzed to yield GDP and the inorganic phosphate ion Pi. Interaction with ribosome enhances GTPase activity of translation factors; i.e., ribosome plays a role of GTPase-activating protein (GAP). GTPases involved in translation interact with ribosome at every stage of protein biosynthesis. Initiation factor 2 (IF2) catalyzes initiator tRNA binding to the ribosome P site and subsequent binding of the 50S subunit to the initiation complex of the 30S subunit. Elongation factor Tu (EF-Tu) controls aminoacyl-tRNA delivery to the ribosome A site, while elongation factor G (EF-G) catalyzes translocation of the mRNA-tRNA complex by one codon on the ribosome. Release factor 3 (RF3) catalyzes the release of termination factors 1 or 2 (RF1 or RF2) from the ribosomal complex after completion of protein synthesis and peptidyl-tRNA hydrolysis. The functional properties of translational GTPases as related to other G-proteins, the putative mechanism of GTP hydrolysis, structural features, and the functional cycles of translational GTPases are considered.

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Authors and Affiliations

  1. Faculty of Chemistry, Moscow State University, Moscow, 119992, Russia

    A. V. Kubarenko & P. V. Sergiev

  2. Institute of Physical Biochemistry, University of Witten/Herdecke, 58448, Witten, Germany

    A. V. Kubarenko & M. V. Rodnina

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  1. A. V. Kubarenko
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  2. P. V. Sergiev
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Translated from Molekulyarnaya Biologiya, Vol. 39, No. 5, 2005, pp. 746–761.

Original Russian Text Copyright © 2005 by Kubarenko, Sergiev, Rodnina.

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Kubarenko, A.V., Sergiev, P.V. & Rodnina, M.V. GTPases of the Translation Apparatus. Mol Biol 39, 646–660 (2005). https://doi.org/10.1007/s11008-005-0080-2

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