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YearIMPACT-FACTOR
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 53(2019) N 4 p. 501-512; DOI 10.1134/S0026893319040034 Full Text

A.A. Golubev1, Sh.Z. Validov1, K.S. Usachev1, M.M. Yusupov1,2*

Elongation Factor P: New Mechanisms of Function and an Evolutionary Diversity of Translation Regulation

1Institute of Fundamental Medicine and Biology, Kazan (Volga) Federal University, Kazan, 420008 Russia
2Institut de Génétique et de Biologie Moléculaire et Cellulaire, Strasbourg, 67404 France

*marat@igbmc.fr
Received - 2019-03-04; Revised - 2019-03-15; Accepted - 2019-03-15

The protein synthesis in cells occurs in ribosomes, with the involvement of protein translational factors. One of these translational factors is the elongation factor P (EF-P). EF-P is a three-domain protein that binds between the P and E sites of the ribosome, near the P-tRNA, the peptidyl transferase center, and E-site codon of the mRNA. The majority of studies showed that the EF-P helps the ribosome to synthesize stalling amino acid motifs, such as polyprolines. In the first part of this review, we inspect the general evolutionary variety of the EF-P in different organisms, the problems of the regulation provided by the EF-P, and its role in the sustainability of the protein balance in the cell in different physiological states. Although the functions of the EF-P have been well studied, there are still some problems that remain to be solved. The data from recent studies contradict the previous theories. Consequently, in the second part, we discuss the recent data that suggest the involvement of the EF-P in each translocation event, not only in those related to poly-proline synthesis. This activity contradicts some aspects of the known pathway of the removal of the E-tRNA during the translocation event. In addition, in the third part of this review, we tried to partly shift the interest from the antistalling activity of domain I of the EF-P to the action of domain III, the functions of which has not been closely studied. We expand on the idea about the involvement of domain III of the EF-P in preventing the frameshift and debate the EF-P's evolutionary history.

ribosome, EF-P, translation



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