Advanced search
Start date
Betweenand


Primary amino acid sequences of decapod (Na plus , K plus )-ATPase provide evolutionary insights into osmoregulatory mechanisms

Full text
Author(s):
Fabri, Leonardo M. ; Moraes, Cintya M. ; Garcon, Daniela P. ; Mcnamara, John C. ; Faria, Samuel C. ; Leone, Francisco A.
Total Authors: 6
Document type: Journal article
Source: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY; v. 296, p. 15-pg., 2024-07-16.
Abstract

Decapod Crustacea exhibit a marine origin, but many taxa have occupied environments ranging from brackish to fresh water and terrestrial habitats, overcoming their inherent osmotic challenges. Osmotic and ionic regulation is achieved by the gill epithelia, driven by two active ATP-hydrolyzing ion transporters, the basal (Na+, K+)ATPase and the apical V(H+)-ATPase. The kinetic characteristic of gill (Na+, K+)-ATPase and the mRNA expression of its alpha subunit have been widely studied in various decapod species under different salinity challenges. However, the evolution of the primary structure has not been explored, especially considering the functional modifications associated with decapod phylogeny. Here, we proposed a model for the topology of the decapod alpha subunit, identifying the sites and motifs involved in its function and regulation, as well as the patterns of its evolution assuming a decapod phylogeny. We also examined both the amino acid substitutions and their functional implications within the context of biochemical and physiological adaptation. The alpha-subunit of decapod crustaceans shows greater conservation (-94% identity) compared to the beta-subunit (-40%). While the binding sites for ATP and modulators are conserved in the decapod enzyme, the residues involved in the alpha-beta interaction are only partially conserved. In the phylogenetic context of the complete sequence of (Na+, K+)ATPase alpha-subunit, most substitutions appear to be characteristic of the entire group, with specific changes for different subgroups, especially among brachyuran crabs. Interestingly, there was no consistent separation of alpha-subunit partial sequences related to habitat, suggesting that the convergent evolution for freshwater or terrestrial modes of life is not correlated with similar changes in the enzyme's primary amino acid sequence. (AU)

FAPESP's process: 22/03105-7 - Using the phylogenetic past to predict climate impacts: ecophysiology of symbiosis and accelerated evolution to coral reef conservation
Grantee:Samuel Coelho de Faria
Support Opportunities: Research Grants - Initial Project
FAPESP's process: 16/25336-0 - Comparative biochemical study of gill (Na+, K +)- ATPase of Macrobrachium amazonicum (Heller, 1862) inhabitant of coastal and continental regions
Grantee:Francisco de Assis Leone
Support Opportunities: Regular Research Grants
FAPESP's process: 19/21899-8 - Kinetic and molecular characterization of the gill (NA+, K+)-ATPase from Macrobrachium amazonicum inhabitants of the Mato Grosso Pantanal and Tocantins-Araguaia River Basin
Grantee:Francisco de Assis Leone
Support Opportunities: Regular Research Grants