A 13 kDa protein, covalently linked to a small RNA from the cytoplasm of mouse cells, was studied. Sequence analysis of its tryptic peptides revealed that the RNA-linked protein is identical to prothymosin a. Very similar RNA-protein complexes were identified in human, bovine and yeast cells. Tryptic peptide maps of 12SI-labelled RNA-linked proteins of diverse origin demonstrated their marked similarity, thus indicating high evolutionary conservation of prothymosin a from yeast to man.Protein-RNA complex; Prothymosin a; Evolutionary conserved protein

A bacterial strain overproducing human prothymosin a was constructed based on the efficient T7 RNA polymerase transcription of human prothymosin a cDNA. The highest yield of the human prothymosin a, up to 30% of the total bacterial protein, was achieved with constructions containing 6-10 nucleotides between the Shine-Dalgarno sequence and initiation ATG codon. Unexpectedly, cells grown in the presence of inducer of T7 RNA polymerase synthesis produced substantially lower levels of prothymosin a than those grown in the absence of inducer. A simple procedure for prothymosin a isolation was elaborated, resulting in large amounts of electrophoretically pure and immunoactive protein.Keywords. Prothymosin a ; Escherichia coli ; immunoactive protein ; T7 RNA polymerase ; protein purification.Prothymosin a is a small highly acidic protein of 13kDa, initially isolated from the rat thymus [I]. Although the thymus is the richest source of prothymosin a, the prothymosin a gene was shown to be expressed in a wide variety of tissues [2]. Moreover, prothymosin a is an evolutionary highly conserved protein from unicellular organisms to man [3].As for prothymosin a function, there are two points of view.First, prothymosin a has been implicated in performing some general function inside the cell; its relation to proliferation has been well documented. High amounts of this protein have been identified in rapidly proliferating mammalian cells, including cancer cells [4]. Serum stimulation of cell division induced transcription of the prothymosin a gene [5]. In accordance with this fact, nuclear oncoprotein MYC appeared to be a positive regulator of prothymosin a gene expression [6]. Blocking of prothymosin a synthesis by antisense oligonucleotides resulted in the inhibition of cell division [7]. Due to the presence of a karyophylic sequence near the carboxy terminus of the molecule, prothymosin a is capable of accumulating in the nucleus [8]. The nuclear localization of prothymosin a was confirmed by immunostaining techniques [9] ; however, some data argued for a cytoplasmic localization of the protein as well [lo], in particular when prothymosin a was covalently linked to a small RNA molecule of unknown origin [3, 111.An alternative view considers prothymosin a as some kind of thymic hormone with immunostimulating properties, or as a precursor of the 28-amino-acid hormone-like peptide thymosin a l , derived from the amino terminus of prothymosin a. appeared to be even more potent than thymosin a1 in the protection of animals against opportunistic infections [13]. Prothymosin a has been demonstrated to promote maturation and differentiation of lymphoid cells, increased production of interleukin-2 and enhanced interleukin-2 receptor expression in human T-lymphocytes [14, 151. Furthermore, treatment with prothymosin a has been reported to promote antitumor activity [16].Whatever the exact function of prothymosin a, further studies and applications require a reliable source of the pure human protein. Here, we report the construction o...

Identtficauon of tile putatwe prothymosin ~ homolo8 in gscherichia colt cells prompted the search for a prothymosm or.coding gone in the E cob genome. A ~ct of interspersed DNA segments was ldenufied, which match various parts of the human prothymosm ~ molecule. Their location in the E coh genome and high degree of simdanty with the appropriate regions of the human prothymosin cc gone suggest that some kind of ttcma.sphcing should e~lst tn £. colt, which could be responsible for bringing these putative bacterial prothymosin a-coding cxons together.

Purpose The system of higher education is ineffective – it has to change the concept of educational process, which is peculiar for increase of the volume of education of labor resources. According to this, there is a necessity to pass to the system of higher education with elements of smart technologies. The purpose of this paper is to determine the role of smart technologies as an innovational and intellectual tool in development of the system of higher education and formation of actual skills with students. Design/methodology/approach The aspects of classical education in universities with elements of remote forms of implementation of smart technologies on IT platforms are studied; peculiarities of smart technology as intellectual tools of higher education are analyzed; perspectives of usage of smart technologies as innovational tools for development of higher education are determined. The research methods include analysis, synthesis, abstraction, comparison and logical method. Findings Information technologies become an inseparable part of life of society and human. A new network generation of people that cannot imagine life without new technological devices is growing. However, despite this, modern education does not sufficiently influence the development of human capital in the conditions of digital environment. Originality/value Scientific novelty consists in conducting the research in the sphere of significance and perspectives of implementing smart technologies into the systems of higher education of the Russian Federation. This paper could be interesting for public officers who form the program of development of higher education and academic staff of higher educational establishments.

A low-molecular-mass RNA from the cytoplasm of mouse Krebs II cells was found to be covalently linked to a protein with an apparent molecular mass of 13 kDa. The protein appears to be attached to the S-terminus of the RNA molecule, which is approx. 20 nucleotides long.small cytoplasmic RNA; RNA-protein complex; Viral protein VPg