Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence
Pseudomonas syringae Lz4W RecBCD enzyme, RecBCDPs, is a trimeric protein complex comprised of RecC, RecB, and RecD subunits. RecBCD enzyme is essential for P. syringae growth at low temperature, and it protects cells from low temperature induced replication arrest. In this study, we show that the Re...
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ftpubmed:oai:pubmedcentral.nih.gov:5959072 2023-05-15T13:46:05+02:00 Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence Pavankumar, Theetha L. Sinha, Anurag K. Ray, Malay K. 2018-05-18 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5959072/ http://www.ncbi.nlm.nih.gov/pubmed/29775464 https://doi.org/10.1371/journal.pone.0197476 en eng Public Library of Science http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5959072/ http://www.ncbi.nlm.nih.gov/pubmed/29775464 http://dx.doi.org/10.1371/journal.pone.0197476 © 2018 Pavankumar et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. CC-BY Research Article Text 2018 ftpubmed https://doi.org/10.1371/journal.pone.0197476 2018-06-03T00:28:44Z Pseudomonas syringae Lz4W RecBCD enzyme, RecBCDPs, is a trimeric protein complex comprised of RecC, RecB, and RecD subunits. RecBCD enzyme is essential for P. syringae growth at low temperature, and it protects cells from low temperature induced replication arrest. In this study, we show that the RecBCDPs enzyme displays distinct biochemical behaviors. Unlike E. coli RecBCD enzyme, the RecD subunit is indispensable for RecBCDPs function. The RecD motor activity is essential for the Chi-like fragments production in P. syringae, highlighting a distinct role for P. syringae RecD subunit in DNA repair and recombination process. Here, we demonstrate that the RecBCDPs enzyme recognizes a unique octameric DNA sequence, 5′-GCTGGCGC-3′ (ChiPs) that attenuates nuclease activity of the enzyme when it enters dsDNA from the 3′-end. We propose that the reduced translocation activities manifested by motor-defective mutants cause cold sensitivity in P. syrinage; emphasizing the importance of DNA processing and recombination functions in rescuing low temperature induced replication fork arrest. Text Antarc* Antarctic PubMed Central (PMC) Antarctic PLOS ONE 13 5 e0197476 |
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Research Article Pavankumar, Theetha L. Sinha, Anurag K. Ray, Malay K. Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
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Research Article |
description |
Pseudomonas syringae Lz4W RecBCD enzyme, RecBCDPs, is a trimeric protein complex comprised of RecC, RecB, and RecD subunits. RecBCD enzyme is essential for P. syringae growth at low temperature, and it protects cells from low temperature induced replication arrest. In this study, we show that the RecBCDPs enzyme displays distinct biochemical behaviors. Unlike E. coli RecBCD enzyme, the RecD subunit is indispensable for RecBCDPs function. The RecD motor activity is essential for the Chi-like fragments production in P. syringae, highlighting a distinct role for P. syringae RecD subunit in DNA repair and recombination process. Here, we demonstrate that the RecBCDPs enzyme recognizes a unique octameric DNA sequence, 5′-GCTGGCGC-3′ (ChiPs) that attenuates nuclease activity of the enzyme when it enters dsDNA from the 3′-end. We propose that the reduced translocation activities manifested by motor-defective mutants cause cold sensitivity in P. syrinage; emphasizing the importance of DNA processing and recombination functions in rescuing low temperature induced replication fork arrest. |
format |
Text |
author |
Pavankumar, Theetha L. Sinha, Anurag K. Ray, Malay K. |
author_facet |
Pavankumar, Theetha L. Sinha, Anurag K. Ray, Malay K. |
author_sort |
Pavankumar, Theetha L. |
title |
Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
title_short |
Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
title_full |
Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
title_fullStr |
Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
title_full_unstemmed |
Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence |
title_sort |
biochemical characterization of recbcd enzyme from an antarctic pseudomonas species and identification of its cognate chi (χ) sequence |
publisher |
Public Library of Science |
publishDate |
2018 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5959072/ http://www.ncbi.nlm.nih.gov/pubmed/29775464 https://doi.org/10.1371/journal.pone.0197476 |
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Antarctic |
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Antarctic |
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Antarc* Antarctic |
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Antarc* Antarctic |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5959072/ http://www.ncbi.nlm.nih.gov/pubmed/29775464 http://dx.doi.org/10.1371/journal.pone.0197476 |
op_rights |
© 2018 Pavankumar et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
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CC-BY |
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https://doi.org/10.1371/journal.pone.0197476 |
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PLOS ONE |
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e0197476 |
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