title: Similarity of the domain structure of proteins as a basis for the conservation of meiosis.
abstract: Meiosis is conserved in all eucaryotic kingdoms, and homologous rows of variability are revealed for the cytological traits of meiosis. To find the nature of these phenomenons, we reviewed the most-studied meiosis-specific proteins and studied them with the methods of bioinformatics. We found that synaptonemal complex proteins have no homology of amino-acid sequence, but are similar in the domain organization and three-dimensional (3D) structure of functionally important domains in budding yeast, nematode, Drosophila, Arabidopsis, and human. Recombination proteins of Rad51/Dmc1 family are conserved to the extent which permits them to make filamentous single-strand deoxyribonucleic acid (ssDNA)-protein intermediates of meiotic recombination. The same structural principles are valid for conservation of the ultrastructure of kinetochores, cell gap contacts, and nuclear pore complexes, such as in the cases when ultrastructure 3D parameters are important for the function. We suggest that self-assembly of protein molecules plays a significant role in building-up of all biological structures mentioned.
authors.affiliation: Vavilov Institute of General Genetics, Russian Academy of Sciences, Moscow, Russian Federation.
authors.forename: Yu F
authors.initials: YF
authors.lastname: Bogdanov
authors.forename: T M
authors.initials: TM
authors.lastname: Grishaeva
authors.forename: S Ya
authors.initials: SY
authors.lastname: Dadashev
mesh_terms: D000818:Animals; D006801:Humans; D008540:Meiosis; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure; D011995:Recombination, Genetic; D040681:Structural Homology, Protein; D013329:Structure-Activity Relationship
chemical_list: D011506:Proteins