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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.

© 2016, Pleiades Publishing, Inc.Staphylococcus aureus is a major opportunistic and versatile pathogen. Because the bacteria rapidly evolve multi-resistances towards antibiotics, there is an urgent need to find novel targets and alternative strategies to cure bacterial infections. Here, we provide a brief overview on the knowledge acquired on S. aureus ribosomes, which is one of the major antibiotic targets. We will show that subtle differences exist between the translation at the initiation step of Gram-negative and Gram-positive bacteria although their ribosomes display a remarkable degree of resemblance. In addition, we will illustrate using specific examples the diversity of mechanisms controlling translation initiation in S. aureus that contribute to shape the expression of the virulence factors in a temporal and dynamic manner.

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First, in joint work with S. Bodine of the University of Puget Sound, Tacoma, Washington, USA, we consider the second-order differential equation e2 y''=(1+e2 ψ(x, e))y with a small parameter e, where ψ is analytic and even with respect to e. It is well known that it has two formal solutions of the form y±(x,e)=e±x/eh±(x,e), where h±(x,e) is a formal series in powers of e whose coefficients are functions of x. It has been shown that one (resp. both) of these solutions are 1-summable in certain directions if ψ satisfies certain conditions, in particular concerning its x-domain. We show that these conditions are essentially necessary for 1-summability of one (resp. both) of the above formal solutions. In the proof, we solve a certain inverse problem: constructing a differential equation corresponding to a certain Stokes phenomenon. The second part of the paper presents joint work with Augustin Fruchard of the University of La Rochelle, France, concerning inverse problems for the general (analytic) linear equations e r y' = A(x,e) y in the neighborhood of a nonturning point and for second-order (analytic) equations e y'' - 2xy'-g(x,e) y=0 exhibiting resonance in the sense of Ackerberg-O'Malley, i.e., satisfying the Matkowsky condition: there exists a nontrivial formal solution $$\hat y\left( {x{\text{, }}\varepsilon } \right) = \sum {y_n } \left( x \right)\varepsilon ^n $$ such that the coefficients have no poles at x=0.