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E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor
Escherichia coli RecBCD is a DNA helicase with two ATPase motors (RecB, a 3′ to 5′ translocase, and RecD, a 5′ to 3′ translocase) that functions in repair of double-stranded DNA breaks. The RecBC heterodimer, with only the RecB motor, remains a processive helicase. Here we examined RecBC translocati...
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Formato: | Texto |
Lenguaje: | English |
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2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2950890/ https://www.ncbi.nlm.nih.gov/pubmed/20852646 http://dx.doi.org/10.1038/nsmb.1901 |
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author | Wu, Colin G. Bradford, Christina Lohman, Timothy M. |
author_facet | Wu, Colin G. Bradford, Christina Lohman, Timothy M. |
author_sort | Wu, Colin G. |
collection | PubMed |
description | Escherichia coli RecBCD is a DNA helicase with two ATPase motors (RecB, a 3′ to 5′ translocase, and RecD, a 5′ to 3′ translocase) that functions in repair of double-stranded DNA breaks. The RecBC heterodimer, with only the RecB motor, remains a processive helicase. Here we examined RecBC translocation along single stranded (ss) DNA. Surprisingly, we find that RecBC displays two translocase activities: the primary translocase moves 3′ to 5′, while the secondary translocase moves RecBC along the opposite strand of a forked DNA at a similar rate. The secondary translocase is insensitive to the ssDNA backbone polarity, and we propose that its function may be to fuel RecBCD translocation along double stranded DNA ahead of the unwinding fork, and to ensure that the unwound single strands move through RecBCD at the same rate after interaction with a Chi sequence. |
format | Text |
id | pubmed-2950890 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
record_format | MEDLINE/PubMed |
spelling | pubmed-29508902011-04-01 E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor Wu, Colin G. Bradford, Christina Lohman, Timothy M. Nat Struct Mol Biol Article Escherichia coli RecBCD is a DNA helicase with two ATPase motors (RecB, a 3′ to 5′ translocase, and RecD, a 5′ to 3′ translocase) that functions in repair of double-stranded DNA breaks. The RecBC heterodimer, with only the RecB motor, remains a processive helicase. Here we examined RecBC translocation along single stranded (ss) DNA. Surprisingly, we find that RecBC displays two translocase activities: the primary translocase moves 3′ to 5′, while the secondary translocase moves RecBC along the opposite strand of a forked DNA at a similar rate. The secondary translocase is insensitive to the ssDNA backbone polarity, and we propose that its function may be to fuel RecBCD translocation along double stranded DNA ahead of the unwinding fork, and to ensure that the unwound single strands move through RecBCD at the same rate after interaction with a Chi sequence. 2010-09-19 2010-10 /pmc/articles/PMC2950890/ /pubmed/20852646 http://dx.doi.org/10.1038/nsmb.1901 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Wu, Colin G. Bradford, Christina Lohman, Timothy M. E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title | E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title_full | E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title_fullStr | E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title_full_unstemmed | E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title_short | E. coli RecBC Helicase has Two Translocase Activities Controlled by a Single ATPase Motor |
title_sort | e. coli recbc helicase has two translocase activities controlled by a single atpase motor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2950890/ https://www.ncbi.nlm.nih.gov/pubmed/20852646 http://dx.doi.org/10.1038/nsmb.1901 |
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