The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/386 |
Resumo: | The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The ?-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the ?-CA family, with an emphasis on metazoan ?-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of ?-CAs, and suggest ?-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO3? ions, a structural protein, a nucleation activator, etc.) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of ?-CAs to diverse metazoan biocalcification processes. An analysis of ?-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans. |
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The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralizationα -Carbonic anhydraseMetazoaBiocalcificationBiomineralizationMolecular evolutionLow complexity domains (LCDs)Repetitive low complexity domains (RLCDs)The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The ?-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the ?-CA family, with an emphasis on metazoan ?-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of ?-CAs, and suggest ?-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO3? ions, a structural protein, a nucleation activator, etc.) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of ?-CAs to diverse metazoan biocalcification processes. An analysis of ?-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans.PhD Fellowship from the Ministère de l' Education Nationale et de la Recherche (contract number 27264–2007), ANR project (ACCRO-Earth, ref. BLAN06-2_159971, coordinator Gilles Ramstein, LSCE, Gif/Yvette, France) for years 2007–2011, SU (INTERRVIE project year 2010), COST network TD0903 "Biomineralix", ECTS (internship grant, 2012).BioMed CentralARCALe Roy, NathalieJackson, Daniel JMarie, BenjaminRamos-Silva, PaulaMarin, Frédéric2015-10-08T10:42:17Z2014-10-172014-10-17T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/386engLe Roy et al. : The evolution of metazoan α -carbonic anhydrases and their roles in calcium carbonate biomineralization. Frontiers in Zoology 2014 11 :75.10.1186/s12983-014-0075-8info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-11-29T14:34:46Zoai:arca.igc.gulbenkian.pt:10400.7/386Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:41.178826Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
title |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
spellingShingle |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization Le Roy, Nathalie α -Carbonic anhydrase Metazoa Biocalcification Biomineralization Molecular evolution Low complexity domains (LCDs) Repetitive low complexity domains (RLCDs) |
title_short |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
title_full |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
title_fullStr |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
title_full_unstemmed |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
title_sort |
The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization |
author |
Le Roy, Nathalie |
author_facet |
Le Roy, Nathalie Jackson, Daniel J Marie, Benjamin Ramos-Silva, Paula Marin, Frédéric |
author_role |
author |
author2 |
Jackson, Daniel J Marie, Benjamin Ramos-Silva, Paula Marin, Frédéric |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
Le Roy, Nathalie Jackson, Daniel J Marie, Benjamin Ramos-Silva, Paula Marin, Frédéric |
dc.subject.por.fl_str_mv |
α -Carbonic anhydrase Metazoa Biocalcification Biomineralization Molecular evolution Low complexity domains (LCDs) Repetitive low complexity domains (RLCDs) |
topic |
α -Carbonic anhydrase Metazoa Biocalcification Biomineralization Molecular evolution Low complexity domains (LCDs) Repetitive low complexity domains (RLCDs) |
description |
The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The ?-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the ?-CA family, with an emphasis on metazoan ?-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of ?-CAs, and suggest ?-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO3? ions, a structural protein, a nucleation activator, etc.) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of ?-CAs to diverse metazoan biocalcification processes. An analysis of ?-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-10-17 2014-10-17T00:00:00Z 2015-10-08T10:42:17Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.7/386 |
url |
http://hdl.handle.net/10400.7/386 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Le Roy et al. : The evolution of metazoan α -carbonic anhydrases and their roles in calcium carbonate biomineralization. Frontiers in Zoology 2014 11 :75. 10.1186/s12983-014-0075-8 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
BioMed Central |
publisher.none.fl_str_mv |
BioMed Central |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799130572216336384 |