Origin and status of homologous proteins of biomineralization (Biosilicification) in the taxonomy of phylogenetic domains

12Citations
Citations of this article
36Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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. © 2013 Igor E. Pamirsky and Kirill S. Golokhvast.

Cite

CITATION STYLE

APA

Pamirsky, I. E., & Golokhvast, K. S. (2013). Origin and status of homologous proteins of biomineralization (Biosilicification) in the taxonomy of phylogenetic domains. BioMed Research International, 2013. https://doi.org/10.1155/2013/397278

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free