Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya
- 567 Downloads
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.
KeywordsSOUL Evolution Heme binding Tetrapyrrole metabolism Light sensing Apoptosis
This research was supported by an SZN-Funded University of Palermo PhD Program and a Travel Grant “Premio Brancaccio 2009” from Lions Club “Megaride” (Napoli, Italy) to AEF. PS is supported by a MIUR PON Grant (PONa3_00239) and a FIRB Grant (RBFR12QW4I). NA is funded through the National Environmental Research Program (NERP), an Australian Government Initiative supporting world class, public good research. The NERP Marine Biodiversity Hub is a collaborative partnership between the University of Tasmania, CSIRO Wealth from Oceans Flagship, Geoscience Australia, Australian Institute of Marine Science, Museum Victoria, Charles Darwin University, and the University of Western Australia (www.nerpmarine.edu.au).
Compliance with Ethical Standards
Conflict of interest
The authors declare that there is no conflict of interest that would prejudice the impartiality of this scientific work.
- Gao JL, Guillabert A, Hu JY, Le YY, Urizar E, Seligman E, Fang KJ, Yuan X, Imbault V, Communi D, Wang JM, Parmentier M, Murphy PM, Migeotte F (2007) F2L, a peptide derived from heme-binding protein, chemoattracts mouse neutrophils by specifically activating Fpr2, the low-affinity N-formylpeptide receptor. J Immunol 178:1450CrossRefPubMedGoogle Scholar
- Hall TA (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp 41:95Google Scholar
- Lee SY, Lee MS, Lee HY, Kim SD, Shim JW, Jo SH, Lee JW, Kim JY, Choi YW, Baek SH, Ryu SH, Bae YS (2008) F2L, a peptide derived from heme-binding protein, inhibits LL-37-induced cell proliferation and tube formation in human umbilical vein endothelial cells. FEBS Lett 582:273CrossRefPubMedGoogle Scholar
- Migeotte I, Riboldi E, Franssen JD, Gregoire F, Loison U, Wittamer V, Detheux M, Robberecht P, Costagliola S, Vassart G, Sozzani S, Parmentier M, Communi D (2005) Identification and characterization of an endogenous chemotactic ligand specific for FPRL2. J Exp Med 201:83CrossRefPubMedPubMedCentralGoogle Scholar
- Oliveira PL, Kawooya JK, Ribeiro JM, Meyer T, Poorman R, Alves EW, Walker FA, Machado EA, Nussenzveig RH, Padovan GJ et al (1995) A heme-binding protein from hemolymph and oocytes of the blood-sucking insect, Rhodnius prolixus. Isolation and characterization. J Biol Chem 270:10897CrossRefPubMedGoogle Scholar
- Rambaut A, Drummond AJ (2007) Tracer v1.4. http://beast.bio.ed.ac.uk/Tracer
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li SM, Albala JS, Lim JH, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005) Towards a proteome-scale map of the human protein–protein interaction network. Nature 437:1173CrossRefPubMedGoogle Scholar
- Szigeti A, Hocsak E, Rapolti E, Racz B, Boronkai A, Pozsgai E, Debreceni B, Bognar Z, Bellyei S, Sumegi B, Gallyas F Jr (2010) Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein. J Biol Chem 285:2140CrossRefPubMedGoogle Scholar