Work

The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization

Year: 2014

Type: article

Abstract: The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The α-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the α-CA family, with an emphasis on metazoan α-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of α-CAs, and suggest α-CA was independently co-opted into a variety of skeleton forming roles ( e.g . as a provider of HCO 3 - ions, a structural protein, a nucleation activator, etc .) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of α-CAs to diverse metazoan biocalcification processes. An analysis of α-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans.

Source: Frontiers in Zoology

DOI: 10.1186/s12983-014-0075-8

Authors: Nathalie Le Roy, Daniel J Jackson, Benjamin Marie, Paula Ramos-Silva, Frédéric Marin