Bioinformatical analysis of Eukaryotic shugoshins revealed meiosis-specific features of vertebrate shugoshins, including human one

• Published in: PeerJ (San Francisco, CA) CA), 2016-11, Vol.4, p.e2736
• Main Authors: Grishaeva, Tatiana M, Kulichenko, Darya, Bogdanov, Yuri F
• Format: Article
• Language: English
• Subjects: Arginine; Chromosomes; Proteins
• ISSN: 2167-8359; 2167-8359
• DOI: 10.7717/peerj.2736

Background Shugoshins (SGOs) are proteins that protect cohesins located at the centromeres of sister chromatids from their early cleavage during mitosis and meiosis in plants, fungi, and animals. Their function is to prevent premature sister-chromatid disjunction and segregation. The study focused on the structural differences among SGOs acting during mitosis and meiosis that cause differences in chromosome behavior in these two types of cell division in different organisms. Methods A bioinformatical analysis of protein domains, conserved amino acid motifs, and physicochemical properties of 32 proteins from 25 species of plants, fungi, and animals was performed. Results We identified a C-terminal amino acid motif that is highly evolutionarily conserved among the SGOs protecting centromere cohesion of sister chromatids in meiotic anaphase I, but not among mitotic SGOs. This meiotic motif is arginine-rich in vertebrates. SGOs differ in different eukaryotic kingdoms by the sets and locations of amino acid motifs and the number of [alpha]-helical regions in the protein molecule. Discussion These structural differences between meiotic and mitotic SGOs probably could be responsible for the prolonged SGOs resistance to degradation during meiotic metaphase I and anaphase I. We suggest that the "arginine comb" in C-end meiotic motifs is capable of interaction by hydrogen bonds with guanine bases in the minor groove of DNA helix, thus protecting SGOs from hydrolysis. Our findings support independent evolution of meiosis in different lineages of multicellular organisms.