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BioMed Research International
Volume 2013, Article ID 397278, 7 pages
Research Article

Origin and Status of Homologous Proteins of Biomineralization (Biosilicification) in the Taxonomy of Phylogenetic Domains

1Analytical Centre of the Mineralogical and Geochemical Researches, Institute of Geology and Nature Management FEB RAS, 1 Relochny Lane, Blagoveshchensk, Russia
2Department of Oil and Gas Deal, Laboratory of Nanotoxicology, Far Eastern Federal University, 37 Pushkinskaya Street, Vladivostok, Russia

Received 1 March 2013; Revised 16 April 2013; Accepted 3 June 2013

Academic Editor: Vassily Lyubetsky

Copyright © 2013 Igor E. Pamirsky and Kirill S. Golokhvast. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The taxonomic affiliation (in the systematisation of viruses, and biological domains) of known peptides and proteins of biomineralization (silicateins, silaffins, silacidins and silicase) and their primary structure homologues were analyzed (methods in silico; using Uniprot database). The total number of known peptides and proteins of biosilicification was counted. The data of the quantitative distribution of the detected homologues found in nature are presented. The similarity of the primary structures of silaffins, silacidins, silicateins, silicase, and their homologues was 21–94%, 45–98%, 39–50%, and 28–40%, respectively. These homologues are found in many organisms, from the Protista to the higher plants and animals, including humans, as well as in bacteria and extracellular agents, and they perform a variety of biological functions, such as biologically controlled mineralisation. The provisional classification of these biomineralization proteins is presented. The interrelation of the origin of the first organic polymers and biomineralization is discussed.