Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.
Identifieur interne : 001D96 ( PubMed/Corpus ); précédent : 001D95; suivant : 001D97Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.
Auteurs : Antonio Emidio Fortunato ; Paolo Sordino ; Nikos AndreakisSource :
- Journal of molecular evolution [ 1432-1432 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Carrier Proteins, Hemeproteins, Tetrapyrroles.
- genetics : Eukaryota, Symbiosis.
- methods : Sequence Alignment.
- Biological Evolution, Databases, Genetic, Evolution, Molecular, Gene Duplication, Phylogeny.
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.
DOI: 10.1007/s00239-016-9745-9
PubMed: 27209522
Links to Exploration step
pubmed:27209522Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.</title><author><name sortKey="Fortunato, Antonio Emidio" sort="Fortunato, Antonio Emidio" uniqKey="Fortunato A" first="Antonio Emidio" last="Fortunato">Antonio Emidio Fortunato</name><affiliation><nlm:affiliation>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.</nlm:affiliation></affiliation></author><author><name sortKey="Sordino, Paolo" sort="Sordino, Paolo" uniqKey="Sordino P" first="Paolo" last="Sordino">Paolo Sordino</name><affiliation><nlm:affiliation>Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Andreakis, Nikos" sort="Andreakis, Nikos" uniqKey="Andreakis N" first="Nikos" last="Andreakis">Nikos Andreakis</name><affiliation><nlm:affiliation>Australian Institute of Marine Science, PMB N° 3, Townsville MC, QLD, 4810, Australia. n.andreakis@gmail.com.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27209522</idno><idno type="pmid">27209522</idno><idno type="doi">10.1007/s00239-016-9745-9</idno><idno type="wicri:Area/PubMed/Corpus">001D96</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001D96</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.</title><author><name sortKey="Fortunato, Antonio Emidio" sort="Fortunato, Antonio Emidio" uniqKey="Fortunato A" first="Antonio Emidio" last="Fortunato">Antonio Emidio Fortunato</name><affiliation><nlm:affiliation>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.</nlm:affiliation></affiliation></author><author><name sortKey="Sordino, Paolo" sort="Sordino, Paolo" uniqKey="Sordino P" first="Paolo" last="Sordino">Paolo Sordino</name><affiliation><nlm:affiliation>Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Andreakis, Nikos" sort="Andreakis, Nikos" uniqKey="Andreakis N" first="Nikos" last="Andreakis">Nikos Andreakis</name><affiliation><nlm:affiliation>Australian Institute of Marine Science, PMB N° 3, Townsville MC, QLD, 4810, Australia. n.andreakis@gmail.com.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of molecular evolution</title><idno type="eISSN">1432-1432</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological Evolution</term><term>Carrier Proteins (genetics)</term><term>Databases, Genetic</term><term>Eukaryota (genetics)</term><term>Evolution, Molecular</term><term>Gene Duplication</term><term>Hemeproteins (genetics)</term><term>Phylogeny</term><term>Sequence Alignment (methods)</term><term>Symbiosis (genetics)</term><term>Tetrapyrroles (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term><term>Hemeproteins</term><term>Tetrapyrroles</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Eukaryota</term><term>Symbiosis</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Evolution</term><term>Databases, Genetic</term><term>Evolution, Molecular</term><term>Gene Duplication</term><term>Phylogeny</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27209522</PMID><DateCreated><Year>2016</Year><Month>06</Month><Day>24</Day></DateCreated><DateCompleted><Year>2017</Year><Month>06</Month><Day>01</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1432</ISSN><JournalIssue CitedMedium="Internet"><Volume>82</Volume><Issue>6</Issue><PubDate><Year>2016</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of molecular evolution</Title><ISOAbbreviation>J. Mol. Evol.</ISOAbbreviation></Journal><ArticleTitle>Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya.</ArticleTitle><Pagination><MedlinePgn>279-90</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00239-016-9745-9</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fortunato</LastName><ForeName>Antonio Emidio</ForeName><Initials>AE</Initials><AffiliationInfo><Affiliation>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.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy. antonio.fortunato@upmc.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sordino</LastName><ForeName>Paolo</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121, Naples, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andreakis</LastName><ForeName>Nikos</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Australian Institute of Marine Science, PMB N° 3, Townsville MC, QLD, 4810, Australia. n.andreakis@gmail.com.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>College of Marine and Environmental Sciences, James Cook University, Townsville, QLD, 4811, Australia. n.andreakis@gmail.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>05</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Mol Evol</MedlineTA><NlmUniqueID>0360051</NlmUniqueID><ISSNLinking>0022-2844</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006420">Hemeproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D045725">Tetrapyrroles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C040231">heme-binding protein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>IUBMB Life. 2007 Aug-Sep;59(8-9):542-51</RefSource><PMID Version="1">17701549</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 2008 Jan 23;582(2):273-8</RefSource><PMID Version="1">18083128</PMID></CommentsCorrections><CommentsCorrections 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UI="D056890" MajorTopicYN="N">Eukaryota</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020440" MajorTopicYN="N">Gene Duplication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006420" MajorTopicYN="N">Hemeproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013559" MajorTopicYN="N">Symbiosis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045725" MajorTopicYN="N">Tetrapyrroles</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Apoptosis</Keyword><Keyword MajorTopicYN="N">Evolution</Keyword><Keyword MajorTopicYN="N">Heme binding</Keyword><Keyword MajorTopicYN="N">Light sensing</Keyword><Keyword MajorTopicYN="N">SOUL</Keyword><Keyword MajorTopicYN="N">Tetrapyrrole metabolism</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>04</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>05</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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