A model for the RecA protein of Mycoplasma synoviae

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 prese...

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Main Authors: Marbella Maria Fonseca, Frank J.B. Alarcon, Ana Tereza de Vasconcelos, Lucymara Fassarela Agnez-Lima
Format: Article
Language:English
Published: Sociedade Brasileira de Genética 2007-01-01
Series:Genetics and Molecular Biology
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018
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author Marbella Maria Fonseca
Frank J.B. Alarcon
Ana Tereza de Vasconcelos
Lucymara Fassarela Agnez-Lima
author_facet Marbella Maria Fonseca
Frank J.B. Alarcon
Ana Tereza de Vasconcelos
Lucymara Fassarela Agnez-Lima
author_sort Marbella Maria Fonseca
collection DOAJ
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.
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spelling doaj.art-1e1dd79bd9f749178e903dc604eee0422022-12-22T01:18:27ZengSociedade Brasileira de GenéticaGenetics and Molecular Biology1415-47571678-46852007-01-0130129029510.1590/S1415-47572007000200018A model for the RecA protein of Mycoplasma synoviaeMarbella Maria FonsecaFrank J.B. AlarconAna Tereza de VasconcelosLucymara Fassarela Agnez-LimaIn 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018DNA repairrecombinationRecAMycoplasma synoviae
spellingShingle Marbella Maria Fonseca
Frank J.B. Alarcon
Ana Tereza de Vasconcelos
Lucymara Fassarela Agnez-Lima
A model for the RecA protein of Mycoplasma synoviae
Genetics and Molecular Biology
DNA repair
recombination
RecA
Mycoplasma synoviae
title 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_short A model for the RecA protein of Mycoplasma synoviae
title_sort model for the reca protein of mycoplasma synoviae
topic DNA repair
recombination
RecA
Mycoplasma synoviae
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000200018
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