Unique arylalkylamine N-acetyltransferase-2 polymorphism in Salmonids and profound variations in thermal stability and catalytic efficiency conferred by two residues

Melatonin contributes to synchronizing major biological and behavioral functions to the cyclic changes in the environment. The arylalkylamine N -acetyltransferase (AANAT) is responsible for a daily rhythm in melatonin secretion. Teleost possess two enzyme forms, AANAT1 and AANAT2, preferentially exp...

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Bibliographic Details
Published in:Journal of Experimental Biology
Main Authors: Cazaméa-Catalan, Damien, Magnanou, Elodie, Helland, Ronny, Besseau, Laurence, Boeuf, Gilles, Falcón, Jack, Jørgensen, Even H.
Format: Text
Language:English
Published: Company of Biologists 2013
Subjects:
Research Article
Arctic
Arctic charr
Global warming
Salvelinus alpinus
Online Access:http://jeb.biologists.org/cgi/content/short/jeb.080960v1
https://doi.org/10.1242/jeb.080960
Description
Summary:Melatonin contributes to synchronizing major biological and behavioral functions to the cyclic changes in the environment. The arylalkylamine N -acetyltransferase (AANAT) is responsible for a daily rhythm in melatonin secretion. Teleost possess two enzyme forms, AANAT1 and AANAT2, preferentially expressed in the retina and pineal organ, respectively. The concomitant action of light and temperature shapes the daily and seasonal changes in melatonin secretion: the former controls duration while the latter modulates amplitude. Investigating the respective roles of light and temperature is particularly relevant in the context of a global warming likely to affect the way fish decode and anticipate seasonal changes with dramatic consequences on their physiology and behavior. Here we investigated the impact of temperature on pineal melatonin secretion of a migratory species, the Arctic charr ( Salvelinus alpinus ), the northernmost living and cold adapted salmonid. We show that temperature impacts directly melatonin production in cultured pineal organs. We also show that one organ expresses two AANAT2 transcripts displaying high similarity between them and with trout Oncorhynchus mykiss AANAT2, differing by only two amino acid sites. We compared the kinetics and 3D models of these enzymes as well as of a chimeric construct, particularly with regard to their response to temperature. Our study brings interesting and totally new information on the evolutionary diversity of AANAT enzymes in Teleost and on the role played by specific residues in the catalytic properties of the enzymes.

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