A model for the RecA protein of Mycoplasma synoviae

Detalhes bibliográficos
Autor(a) principal: Fonseca,Marbella Maria
Data de Publicação: 2007
Outros Autores: Alarcon,Frank J.B., Vasconcelos,Ana Tereza de, Agnez-Lima,Lucymara Fassarela
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Genetics and Molecular Biology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018
Resumo: In this work, we predict a structural model for the RecA protein from M. synoviae (MsRecA) by theoretical homology modeling and evaluate the occurrence of polymorphisms in this protein within several isolates of this species. The structural model suggested for MsRecA conserves the main domains present in MtRecA and EcRecA. The L1 and L2 regions showed six and three amino acid substitutions, respectively, which apparently do not affect the conformation and function of MsRecA. The C-terminal domain is shorter than that found in EcRecA and MtRecA, which may increase its capacity to bind dsDNA and displace SSB, compensating the absence of recombination initiation enzymes. The MS59 isolate RecA sequence showed one polymorphism which does not affect its functions since these belong to the same physical-chemical group.
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spelling A model for the RecA protein of Mycoplasma synoviaeDNA repairrecombinationRecAMycoplasma synoviaeIn this work, we predict a structural model for the RecA protein from M. synoviae (MsRecA) by theoretical homology modeling and evaluate the occurrence of polymorphisms in this protein within several isolates of this species. The structural model suggested for MsRecA conserves the main domains present in MtRecA and EcRecA. The L1 and L2 regions showed six and three amino acid substitutions, respectively, which apparently do not affect the conformation and function of MsRecA. The C-terminal domain is shorter than that found in EcRecA and MtRecA, which may increase its capacity to bind dsDNA and displace SSB, compensating the absence of recombination initiation enzymes. The MS59 isolate RecA sequence showed one polymorphism which does not affect its functions since these belong to the same physical-chemical group.Sociedade Brasileira de Genética2007-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018Genetics and Molecular Biology v.30 n.1 suppl.0 2007reponame:Genetics and Molecular Biologyinstname:Sociedade Brasileira de Genética (SBG)instacron:SBG10.1590/S1415-47572007000200018info:eu-repo/semantics/openAccessFonseca,Marbella MariaAlarcon,Frank J.B.Vasconcelos,Ana Tereza deAgnez-Lima,Lucymara Fassarelaeng2007-05-14T00:00:00Zoai:scielo:S1415-47572007000200018Revistahttp://www.gmb.org.br/ONGhttps://old.scielo.br/oai/scielo-oai.php||editor@gmb.org.br1678-46851415-4757opendoar:2007-05-14T00:00Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)false
dc.title.none.fl_str_mv A model for the RecA protein of Mycoplasma synoviae
title A model for the RecA protein of Mycoplasma synoviae
spellingShingle A model for the RecA protein of Mycoplasma synoviae
Fonseca,Marbella Maria
DNA repair
recombination
RecA
Mycoplasma synoviae
title_short A model for the RecA protein of Mycoplasma synoviae
title_full A model for the RecA protein of Mycoplasma synoviae
title_fullStr A model for the RecA protein of Mycoplasma synoviae
title_full_unstemmed A model for the RecA protein of Mycoplasma synoviae
title_sort A model for the RecA protein of Mycoplasma synoviae
author Fonseca,Marbella Maria
author_facet Fonseca,Marbella Maria
Alarcon,Frank J.B.
Vasconcelos,Ana Tereza de
Agnez-Lima,Lucymara Fassarela
author_role author
author2 Alarcon,Frank J.B.
Vasconcelos,Ana Tereza de
Agnez-Lima,Lucymara Fassarela
author2_role author
author
author
dc.contributor.author.fl_str_mv Fonseca,Marbella Maria
Alarcon,Frank J.B.
Vasconcelos,Ana Tereza de
Agnez-Lima,Lucymara Fassarela
dc.subject.por.fl_str_mv DNA repair
recombination
RecA
Mycoplasma synoviae
topic DNA repair
recombination
RecA
Mycoplasma synoviae
description In this work, we predict a structural model for the RecA protein from M. synoviae (MsRecA) by theoretical homology modeling and evaluate the occurrence of polymorphisms in this protein within several isolates of this species. The structural model suggested for MsRecA conserves the main domains present in MtRecA and EcRecA. The L1 and L2 regions showed six and three amino acid substitutions, respectively, which apparently do not affect the conformation and function of MsRecA. The C-terminal domain is shorter than that found in EcRecA and MtRecA, which may increase its capacity to bind dsDNA and displace SSB, compensating the absence of recombination initiation enzymes. The MS59 isolate RecA sequence showed one polymorphism which does not affect its functions since these belong to the same physical-chemical group.
publishDate 2007
dc.date.none.fl_str_mv 2007-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1415-47572007000200018
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Genética
publisher.none.fl_str_mv Sociedade Brasileira de Genética
dc.source.none.fl_str_mv Genetics and Molecular Biology v.30 n.1 suppl.0 2007
reponame:Genetics and Molecular Biology
instname:Sociedade Brasileira de Genética (SBG)
instacron:SBG
instname_str Sociedade Brasileira de Genética (SBG)
instacron_str SBG
institution SBG
reponame_str Genetics and Molecular Biology
collection Genetics and Molecular Biology
repository.name.fl_str_mv Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)
repository.mail.fl_str_mv ||editor@gmb.org.br
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