Molecular evolution of the proopiomelanocortin system in Barn owl species.

Details

Serval ID
serval:BIB_31BFEB471ECA
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Molecular evolution of the proopiomelanocortin system in Barn owl species.
Journal
PloS one
Author(s)
Löw K., Ducrest A.L., San-Jose L.M., Simon C., Uva V., Seidah N.G., Pasquato A., Kunz S., Roulin A.
ISSN
1932-6203 (Electronic)
ISSN-L
1932-6203
Publication state
Published
Issued date
2020
Peer-reviewed
Oui
Volume
15
Number
5
Pages
e0231163
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Abstract
Examination of genetic polymorphisms in outbred wild-living species provides insights into the evolution of complex systems. In higher vertebrates, the proopiomelanocortin (POMC) precursor gives rise to α-, β-, and γ-melanocyte-stimulating hormones (MSH), which are involved in numerous physiological aspects. Genetic defects in POMC are linked to metabolic disorders in humans and animals. In the present study, we undertook an evolutionary genetic approach complemented with biochemistry to investigate the functional consequences of genetic polymorphisms in the POMC system of free-living outbred barn owl species (family Tytonidae) at the molecular level. Our phylogenetic studies revealed a striking correlation between a loss-of-function H9P mutation in the β-MSH receptor-binding motif and an extension of a poly-serine stretch in γ3-MSH to ≥7 residues that arose in the barn owl group 6-8 MYA ago. We found that extension of the poly-serine stretches in the γ-MSH locus affects POMC precursor processing, increasing γ3-MSH production at the expense of γ2-MSH and resulting in an overall reduction of γ-MSH signaling, which may be part of a negative feedback mechanism. Extension of the γ3-MSH poly-serine stretches ≥7 further markedly increases peptide hormone stability in plasma, which is conserved in humans, and is likely relevant to its endocrine function. In sum, our phylogenetic analysis of POMC in wild living owls uncovered a H9P β-MSH mutation subsequent to serine extension in γ3-MSH to 7 residues, which was then followed by further serine extension. The linked MSH mutations highlight the genetic plasticity enabled by the modular design of the POMC gene.
Keywords
Amino Acid Motifs, Animals, Animals, Outbred Strains, Binding Sites, Evolution, Molecular, Feedback, Physiological, Genotyping Techniques/veterinary, Loss of Function Mutation, Microsatellite Repeats, Phylogeny, Pro-Opiomelanocortin/chemistry, Pro-Opiomelanocortin/genetics, Pro-Opiomelanocortin/metabolism, Protein Stability, Signal Transduction, Strigiformes/classification, Strigiformes/genetics, Strigiformes/metabolism, Tissue Distribution
Pubmed
Web of science
Open Access
Yes
Create date
16/06/2020 14:43
Last modification date
10/10/2020 5:26
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