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Purpose: Actuality of this subject is predetermined by the fact that global competitiveness and expansion of exchange of knowledge made employers not only increase requirements to factual results of the study at all levels of education but also announce the necessity of formation of new qualities with graduates. The purpose of this paper is to develop a complex of recommendations for employers' participation in the formation of educational programs for preparing specialists in the service sphere, aimed at improving education quality and the demand for graduates in the labor market. Design/methodology/approach: A method which leads to the study of this problem is desk methods of research. For an evaluation of the results of realization of educational programs and use of educational resources for training of specialists in the service sphere, the authors conducted a survey of employers (representatives of service sphere); the selection constituted 300 people. Findings: The paper determines scientifically substantiated directions of activities for the participation of employers in the formation of educational programs and resources for training of specialists in the service sphere. The authors developed a model of interconnection of purposes and results of employers' participation in the realization of educational programs, formation, and use of educational resources. Originality/value: The practical significance of this research consists in the fact that received results and offers could be used by educational establishments, employers, and professional associations.

A powder-filled epoxy compound was tested for cavitation wear in the form of bronze particles BraZHNMc9-4-4-1. The particles were obtained by sawing a bronze bar. The composition of the compound was as follows: 100 parts of resin K-153 and 12 parts of hardener (polyethylene polyamine). The specimens were shaped as cylinders, 15.5 and 15 mm in diameter and height, respectively. The tests were carried out with an ultrasonic magnetostrictive vibrator in fresh water at water temperature 20 ± 3 ° C. The frequency and amplitude of oscillations of the vibrator hub end were approximately 22 kHz and 28 μm, respectively. The distance between the end of the concentrator and the end of the specimen wear was set to 0.5 mm. A second-order model describing the cavitation wear as a function of the bronze particle size, its content in the composite and the specific surface area of the particles was constructed by the least-squares method. The cavitation wear of the composite increases with increasing values of these parameters. The greatest influence on composite cavitation wear has the total surface area of bronze microparticles in volume unit.

Simple Summary: Prions are self-perpetuating protein aggregates that cause fatal neurodegenerative diseases in humans and other mammalian species. In yeast, in contrast to mammals, prions can be maintained in the cell population and confer adaptive traits. Fluorescence microscopy is commonly used to visualize prion aggregates in living cells, providing important information regarding the morphology and localization of prion particles in the cell. In most studies, various constructs with green fluorescent protein (GFP) are used to detect particles of the most-studied yeast prion, [PSI+]. In our work, we tried to substitute GFP with two different red fluorescent protein variants to expand the application of prion particle imaging. Surprisingly, we found that the processing of the fluorescently labeled prionogenic protein can prevent the detection of prion particles. This pattern was observed for one of the studied red fluorescent proteins (mCherry) and was not dependent on any tested protein degradation systems. The present work thus highlights the limitations of aggregate labeling with fluorescent proteins and suggests labeling with mCherry should be avoided. Yeast is a convenient model for studying protein aggregation as it is known to propagate amyloid prions. [PSI+] is the prion form of the release factor eRF3 (Sup35). Aggregated Sup35 causes defects in termination of translation, which results in nonsense suppression in strains carrying premature stop codons. N-terminal and middle (M) domains of Sup35 are necessary and sufficient for maintaining [PSI+] in cells while preserving the prion strain's properties. For this reason, Sup35NM fused to fluorescent proteins is often used for [PSI+] detection and investigation. However, we found that in such chimeric constructs, not all fluorescent proteins allow the reliable detection of Sup35 aggregates. Particularly, transient overproduction of Sup35NM-mCherry resulted in a diffuse fluorescent pattern in the [PSI+] cells, while no loss of prions and no effect on the Sup35NM prion properties could be observed. This effect was reproduced in various unrelated strain backgrounds and prion variants. In contrast, Sup35NM fused to another red fluorescent protein, TagRFP-T, allowed the detection of [PSI+] aggregates. Analysis of protein lysates showed that Sup35NM-mCherry is actively degraded in the cell. This degradation was not caused by vacuolar proteases and the ubiquitin-proteasomal system implicated in the Sup35 processing. Even though the intensity of this proteolysis was higher than that of Sup35NM-GFP, it was roughly the same as in the case of Sup35NM-TagRFP-T. Thus, it is possible that, in contrast to TagRFP-T, degradation products of Sup35NM-mCherry still preserve their fluorescent properties while losing the ability to decorate pre-existing Sup35 aggregates. This results in diffuse fluorescence despite the presence of the prion aggregates in the cell. Thus, tagging with fluorescent proteins should be used with caution, as such proteolysis may increase the rate of false-negative results when detecting prion-bearing cells. [ABSTRACT FROM AUTHOR]