Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins

Autores
Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Echave, Julián
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We studied the evolutionary relationships between γ-carbonic anhydrase (γ-CA) and a very diverse group of proteins that share the sequence motif characteristic of the left-handed parallel β-helix (LβH) fold. This sequence motif is characterized by the imperfect tandem repetition of short hexapeptide units, which makes it difficult to obtain a reliable alignment based on sequence information alone. To solve this problem, we used a structural alignment of three members of the group with known crystallographic structures as a seed to obtain a reliable sequence alignment. Then, we applied protein maximum-parsimony and maximum-likelihood phylogenetic inference methods to this alignment. We found that γ-CA belongs to a diverse superfamily of proteins that share the LβH domain. This superfamily is composed mainly of acyltransferases. The most remarkable feature of the phylogenetic tree obtained is that its main branches group together functionally related proteins, so that the coarse topology can be rather easily explained in terms of functional diversification. Regarding the main branch of the tree containing γ-CA, we found that, in addition to the group of its closest relatives that had already been studied, γ-CA is closely related to the tetrahydrodipicolinate N-succinyltransferases. (C) 2000 Academic Press.
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Echave, Julián. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Protein Evolution
Gamma Carbonic Anhydrase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/71608
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related ProteinsParisi, Gustavo DanielFornasari, Maria SilvinaEchave, JuliánProtein EvolutionGamma Carbonic Anhydrasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We studied the evolutionary relationships between γ-carbonic anhydrase (γ-CA) and a very diverse group of proteins that share the sequence motif characteristic of the left-handed parallel β-helix (LβH) fold. This sequence motif is characterized by the imperfect tandem repetition of short hexapeptide units, which makes it difficult to obtain a reliable alignment based on sequence information alone. To solve this problem, we used a structural alignment of three members of the group with known crystallographic structures as a seed to obtain a reliable sequence alignment. Then, we applied protein maximum-parsimony and maximum-likelihood phylogenetic inference methods to this alignment. We found that γ-CA belongs to a diverse superfamily of proteins that share the LβH domain. This superfamily is composed mainly of acyltransferases. The most remarkable feature of the phylogenetic tree obtained is that its main branches group together functionally related proteins, so that the coarse topology can be rather easily explained in terms of functional diversification. Regarding the main branch of the tree containing γ-CA, we found that, in addition to the group of its closest relatives that had already been studied, γ-CA is closely related to the tetrahydrodipicolinate N-succinyltransferases. (C) 2000 Academic Press.Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Echave, Julián. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAcademic Press Inc Elsevier Science2000-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/71608Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Echave, Julián; Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 14; 3; 12-2000; 323-3341055-7903CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1006/mpev.1999.0734info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1055790399907340info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:18:06Zoai:ri.conicet.gov.ar:11336/71608instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:18:06.491CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
title Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
spellingShingle Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
Parisi, Gustavo Daniel
Protein Evolution
Gamma Carbonic Anhydrase
title_short Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
title_full Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
title_fullStr Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
title_full_unstemmed Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
title_sort Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins
dc.creator.none.fl_str_mv Parisi, Gustavo Daniel
Fornasari, Maria Silvina
Echave, Julián
author Parisi, Gustavo Daniel
author_facet Parisi, Gustavo Daniel
Fornasari, Maria Silvina
Echave, Julián
author_role author
author2 Fornasari, Maria Silvina
Echave, Julián
author2_role author
author
dc.subject.none.fl_str_mv Protein Evolution
Gamma Carbonic Anhydrase
topic Protein Evolution
Gamma Carbonic Anhydrase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We studied the evolutionary relationships between γ-carbonic anhydrase (γ-CA) and a very diverse group of proteins that share the sequence motif characteristic of the left-handed parallel β-helix (LβH) fold. This sequence motif is characterized by the imperfect tandem repetition of short hexapeptide units, which makes it difficult to obtain a reliable alignment based on sequence information alone. To solve this problem, we used a structural alignment of three members of the group with known crystallographic structures as a seed to obtain a reliable sequence alignment. Then, we applied protein maximum-parsimony and maximum-likelihood phylogenetic inference methods to this alignment. We found that γ-CA belongs to a diverse superfamily of proteins that share the LβH domain. This superfamily is composed mainly of acyltransferases. The most remarkable feature of the phylogenetic tree obtained is that its main branches group together functionally related proteins, so that the coarse topology can be rather easily explained in terms of functional diversification. Regarding the main branch of the tree containing γ-CA, we found that, in addition to the group of its closest relatives that had already been studied, γ-CA is closely related to the tetrahydrodipicolinate N-succinyltransferases. (C) 2000 Academic Press.
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Echave, Julián. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description We studied the evolutionary relationships between γ-carbonic anhydrase (γ-CA) and a very diverse group of proteins that share the sequence motif characteristic of the left-handed parallel β-helix (LβH) fold. This sequence motif is characterized by the imperfect tandem repetition of short hexapeptide units, which makes it difficult to obtain a reliable alignment based on sequence information alone. To solve this problem, we used a structural alignment of three members of the group with known crystallographic structures as a seed to obtain a reliable sequence alignment. Then, we applied protein maximum-parsimony and maximum-likelihood phylogenetic inference methods to this alignment. We found that γ-CA belongs to a diverse superfamily of proteins that share the LβH domain. This superfamily is composed mainly of acyltransferases. The most remarkable feature of the phylogenetic tree obtained is that its main branches group together functionally related proteins, so that the coarse topology can be rather easily explained in terms of functional diversification. Regarding the main branch of the tree containing γ-CA, we found that, in addition to the group of its closest relatives that had already been studied, γ-CA is closely related to the tetrahydrodipicolinate N-succinyltransferases. (C) 2000 Academic Press.
publishDate 2000
dc.date.none.fl_str_mv 2000-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/71608
Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Echave, Julián; Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 14; 3; 12-2000; 323-334
1055-7903
CONICET Digital
CONICET
url http://hdl.handle.net/11336/71608
identifier_str_mv Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Echave, Julián; Evolutionary Analysis of -Carbonic Anhydrase and Structurally Related Proteins; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 14; 3; 12-2000; 323-334
1055-7903
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1006/mpev.1999.0734
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1055790399907340
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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