Evolution based on domain combinations: the case of glutaredoxins.
Identifieur interne : 000B30 ( Main/Exploration ); précédent : 000B29; suivant : 000B31Evolution based on domain combinations: the case of glutaredoxins.
Auteurs : Rui Alves [Espagne] ; Ester Vilaprinyo ; Albert Sorribas ; Enrique HerreroSource :
- BMC evolutionary biology [ 1471-2148 ] ; 2009.
Descripteurs français
- KwdFr :
- Algorithmes (MeSH), Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Animaux (MeSH), Archéobactéries (génétique), Bactéries (génétique), Glutarédoxines (génétique), Phylogenèse (MeSH), Recombinaison génétique (génétique), Structure tertiaire des protéines (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Évolution moléculaire (MeSH).
- MESH :
English descriptors
- KwdEn :
- Algorithms (MeSH), Amino Acid Sequence (MeSH), Animals (MeSH), Archaea (genetics), Bacteria (genetics), Conserved Sequence (MeSH), Evolution, Molecular (MeSH), Glutaredoxins (genetics), Phylogeny (MeSH), Protein Structure, Tertiary (MeSH), Recombination, Genetic (genetics), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH).
- MESH :
- chemical , genetics : Glutaredoxins.
- genetics : Archaea, Bacteria, Recombination, Genetic.
- Algorithms, Amino Acid Sequence, Animals, Conserved Sequence, Evolution, Molecular, Phylogeny, Protein Structure, Tertiary, Sequence Alignment, Sequence Analysis, Protein.
Abstract
BACKGROUND
Protein domains represent the basic units in the evolution of proteins. Domain duplication and shuffling by recombination and fusion, followed by divergence are the most common mechanisms in this process. Such domain fusion and recombination events are predicted to occur only once for a given multidomain architecture. However, other scenarios may be relevant in the evolution of specific proteins, such as convergent evolution of multidomain architectures. With this in mind, we study glutaredoxin (GRX) domains, because these domains of approximately one hundred amino acids are widespread in archaea, bacteria and eukaryotes and participate in fusion proteins. GRXs are responsible for the reduction of protein disulfides or glutathione-protein mixed disulfides and are involved in cellular redox regulation, although their specific roles and targets are often unclear.
RESULTS
In this work we analyze the distribution and evolution of GRX proteins in archaea, bacteria and eukaryotes. We study over one thousand GRX proteins, each containing at least one GRX domain, from hundreds of different organisms and trace the origin and evolution of the GRX domain within the tree of life.
CONCLUSION
Our results suggest that single domain GRX proteins of the CGFS and CPYC classes have, each, evolved through duplication and divergence from one initial gene that was present in the last common ancestor of all organisms. Remarkably, we identify a case of convergent evolution in domain architecture that involves the GRX domain. Two independent recombination events of a TRX domain to a GRX domain are likely to have occurred, which is an exception to the dominant mechanism of domain architecture evolution.
DOI: 10.1186/1471-2148-9-66
PubMed: 19321008
PubMed Central: PMC2679010
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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wicri:level="1"><nlm:affiliation>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, Lleida, Spain. ralves@cmb.udl.es</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, Lleida</wicri:regionArea><wicri:noRegion>Lleida</wicri:noRegion></affiliation></author><author><name sortKey="Vilaprinyo, Ester" sort="Vilaprinyo, Ester" uniqKey="Vilaprinyo E" first="Ester" last="Vilaprinyo">Ester Vilaprinyo</name></author><author><name sortKey="Sorribas, Albert" sort="Sorribas, Albert" uniqKey="Sorribas A" first="Albert" last="Sorribas">Albert Sorribas</name></author><author><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name></author></analytic><series><title level="j">BMC evolutionary biology</title><idno type="eISSN">1471-2148</idno><imprint><date when="2009" 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génétique (génétique)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Archaea</term><term>Bacteria</term><term>Recombination, Genetic</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Archéobactéries</term><term>Bactéries</term><term>Glutarédoxines</term><term>Recombinaison génétique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Algorithms</term><term>Amino Acid Sequence</term><term>Animals</term><term>Conserved Sequence</term><term>Evolution, Molecular</term><term>Phylogeny</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Sequence Analysis, Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Algorithmes</term><term>Alignement de séquences</term><term>Analyse de séquence de protéine</term><term>Animaux</term><term>Phylogenèse</term><term>Structure tertiaire des protéines</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Protein domains represent the basic units in the evolution of proteins. Domain duplication and shuffling by recombination and fusion, followed by divergence are the most common mechanisms in this process. Such domain fusion and recombination events are predicted to occur only once for a given multidomain architecture. However, other scenarios may be relevant in the evolution of specific proteins, such as convergent evolution of multidomain architectures. With this in mind, we study glutaredoxin (GRX) domains, because these domains of approximately one hundred amino acids are widespread in archaea, bacteria and eukaryotes and participate in fusion proteins. GRXs are responsible for the reduction of protein disulfides or glutathione-protein mixed disulfides and are involved in cellular redox regulation, although their specific roles and targets are often unclear.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>In this work we analyze the distribution and evolution of GRX proteins in archaea, bacteria and eukaryotes. We study over one thousand GRX proteins, each containing at least one GRX domain, from hundreds of different organisms and trace the origin and evolution of the GRX domain within the tree of life.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>Our results suggest that single domain GRX proteins of the CGFS and CPYC classes have, each, evolved through duplication and divergence from one initial gene that was present in the last common ancestor of all organisms. Remarkably, we identify a case of convergent evolution in domain architecture that involves the GRX domain. Two independent recombination events of a TRX domain to a GRX domain are likely to have occurred, which is an exception to the dominant mechanism of domain architecture evolution.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19321008</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1471-2148</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><PubDate><Year>2009</Year><Month>Mar</Month><Day>25</Day></PubDate></JournalIssue><Title>BMC evolutionary biology</Title><ISOAbbreviation>BMC Evol Biol</ISOAbbreviation></Journal><ArticleTitle>Evolution based on domain combinations: the case of glutaredoxins.</ArticleTitle><Pagination><MedlinePgn>66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/1471-2148-9-66</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Protein domains represent the basic units in the evolution of proteins. Domain duplication and shuffling by recombination and fusion, followed by divergence are the most common mechanisms in this process. Such domain fusion and recombination events are predicted to occur only once for a given multidomain architecture. However, other scenarios may be relevant in the evolution of specific proteins, such as convergent evolution of multidomain architectures. With this in mind, we study glutaredoxin (GRX) domains, because these domains of approximately one hundred amino acids are widespread in archaea, bacteria and eukaryotes and participate in fusion proteins. GRXs are responsible for the reduction of protein disulfides or glutathione-protein mixed disulfides and are involved in cellular redox regulation, although their specific roles and targets are often unclear.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">In this work we analyze the distribution and evolution of GRX proteins in archaea, bacteria and eukaryotes. We study over one thousand GRX proteins, each containing at least one GRX domain, from hundreds of different organisms and trace the origin and evolution of the GRX domain within the tree of life.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">Our results suggest that single domain GRX proteins of the CGFS and CPYC classes have, each, evolved through duplication and divergence from one initial gene that was present in the last common ancestor of all organisms. Remarkably, we identify a case of convergent evolution in domain architecture that involves the GRX domain. 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sortKey="Sorribas, Albert" sort="Sorribas, Albert" uniqKey="Sorribas A" first="Albert" last="Sorribas">Albert Sorribas</name><name sortKey="Vilaprinyo, Ester" sort="Vilaprinyo, Ester" uniqKey="Vilaprinyo E" first="Ester" last="Vilaprinyo">Ester Vilaprinyo</name></noCountry><country name="Espagne"><noRegion><name sortKey="Alves, Rui" sort="Alves, Rui" uniqKey="Alves R" first="Rui" last="Alves">Rui Alves</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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