The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae
DNA repair is crucial to the survival of all organisms. The bacterial RecA protein is a central component in the SOS response and in recombinational and SOS DNA repairs. The RecX protein has been characterized as a negative modulator of RecA activity in many bacteria. The recA and recX genes of Herb...
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2012-12-01
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| Series: | Brazilian Journal of Medical and Biological Research |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012001200004 |
| _version_ | 1828467599190523904 |
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| author | C.W. Galvão E.M. Souza R.M. Etto F.O. Pedrosa L.S. Chubatsu M.G. Yates J. Schumacher M. Buck M.B.R. Steffens |
| author_facet | C.W. Galvão E.M. Souza R.M. Etto F.O. Pedrosa L.S. Chubatsu M.G. Yates J. Schumacher M. Buck M.B.R. Steffens |
| author_sort | C.W. Galvão |
| collection | DOAJ |
| description | DNA repair is crucial to the survival of all organisms. The bacterial RecA protein is a central component in the SOS response and in recombinational and SOS DNA repairs. The RecX protein has been characterized as a negative modulator of RecA activity in many bacteria. The recA and recX genes of Herbaspirillum seropedicae constitute a single operon, and evidence suggests that RecX participates in SOS repair. In the present study, we show that the H. seropedicae RecX protein (RecX Hs) can interact with the H. seropedicaeRecA protein (RecA Hs) and that RecA Hs possesses ATP binding, ATP hydrolyzing and DNA strand exchange activities. RecX Hs inhibited 90% of the RecA Hs DNA strand exchange activity even when present in a 50-fold lower molar concentration than RecA Hs. RecA Hs ATP binding was not affected by the addition of RecX, but the ATPase activity was reduced. When RecX Hs was present before the formation of RecA filaments (RecA-ssDNA), inhibition of ATPase activity was substantially reduced and excess ssDNA also partially suppressed this inhibition. The results suggest that the RecX Hs protein negatively modulates the RecA Hs activities by protein-protein interactions and also by DNA-protein interactions. |
| first_indexed | 2024-12-11T04:08:42Z |
| format | Article |
| id | doaj.art-75cb2ce319fd48a7a310cada487be934 |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-11T04:08:42Z |
| publishDate | 2012-12-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-75cb2ce319fd48a7a310cada487be9342022-12-22T01:21:27ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2012-12-01451211271134The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicaeC.W. GalvãoE.M. SouzaR.M. EttoF.O. PedrosaL.S. ChubatsuM.G. YatesJ. SchumacherM. BuckM.B.R. SteffensDNA repair is crucial to the survival of all organisms. The bacterial RecA protein is a central component in the SOS response and in recombinational and SOS DNA repairs. The RecX protein has been characterized as a negative modulator of RecA activity in many bacteria. The recA and recX genes of Herbaspirillum seropedicae constitute a single operon, and evidence suggests that RecX participates in SOS repair. In the present study, we show that the H. seropedicae RecX protein (RecX Hs) can interact with the H. seropedicaeRecA protein (RecA Hs) and that RecA Hs possesses ATP binding, ATP hydrolyzing and DNA strand exchange activities. RecX Hs inhibited 90% of the RecA Hs DNA strand exchange activity even when present in a 50-fold lower molar concentration than RecA Hs. RecA Hs ATP binding was not affected by the addition of RecX, but the ATPase activity was reduced. When RecX Hs was present before the formation of RecA filaments (RecA-ssDNA), inhibition of ATPase activity was substantially reduced and excess ssDNA also partially suppressed this inhibition. The results suggest that the RecX Hs protein negatively modulates the RecA Hs activities by protein-protein interactions and also by DNA-protein interactions.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012001200004RecARecXHerbaspirillum seropedicaeSOS repair |
| spellingShingle | C.W. Galvão E.M. Souza R.M. Etto F.O. Pedrosa L.S. Chubatsu M.G. Yates J. Schumacher M. Buck M.B.R. Steffens The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae Brazilian Journal of Medical and Biological Research RecA RecX Herbaspirillum seropedicae SOS repair |
| title | The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae |
| title_full | The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae |
| title_fullStr | The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae |
| title_full_unstemmed | The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae |
| title_short | The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae |
| title_sort | recx protein interacts with the reca protein and modulates its activity in herbaspirillum seropedicae |
| topic | RecA RecX Herbaspirillum seropedicae SOS repair |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012001200004 |
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