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J Mol Evol. 2016 Jun;82(6):279-90. doi: 10.1007/s00239-016-9745-9. Epub 2016 May 21.

Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.

Author information

1
Sorbonne Universités, UPMC, Institut de Biologie Paris-Seine, CNRS, Laboratoire de Biologie Computationnelle et Quantitative UMR 7238, 15 rue de l'Ecole de Médecine, 75006, Paris, France. antonio.fortunato@upmc.fr.
2
Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy. antonio.fortunato@upmc.fr.
3
Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy.
4
Australian Institute of Marine Science, PMB N° 3, Townsville MC, QLD, 4810, Australia. n.andreakis@gmail.com.
5
College of Marine and Environmental Sciences, James Cook University, Townsville, QLD, 4811, Australia. n.andreakis@gmail.com.

Abstract

SOUL homologs constitute a heme-binding protein superfamily putatively involved in heme and tetrapyrrole metabolisms associated with a number of physiological processes. Despite their omnipresence across the tree of life and the biochemical characterization of many SOUL members, their functional role and the evolutionary events leading to such remarkable protein repertoire still remain cryptic. To explore SOUL evolution, we apply a computational phylogenetic approach, including a relevant number of SOUL homologs, to identify paralog forms and reconstruct their genealogy across the tree of life and within species. In animal lineages, multiple gene duplication or loss events and paralog functional specializations underlie SOUL evolution from the dawn of ancestral echinoderm and mollusc SOUL forms. In photosynthetic organisms, SOUL evolution is linked to the endosymbiosis events leading to plastid acquisition in eukaryotes. Derivative features, such as the F2L peptide and BH3 domain, evolved in vertebrates and provided innovative functionality to support immune response and apoptosis. The evolution of elements such as the N-terminal protein domain DUF2358, the His42 residue, or the tetrapyrrole heme-binding site is modern, and their functional implications still unresolved. This study represents the first in-depth analysis of SOUL protein evolution and provides novel insights in the understanding of their obscure physiological role.

KEYWORDS:

Apoptosis; Evolution; Heme binding; Light sensing; SOUL; Tetrapyrrole metabolism

PMID:
27209522
DOI:
10.1007/s00239-016-9745-9
[Indexed for MEDLINE]

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