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DNA sliding and loop formation by E. coli SMC complex: MukBEF
SMC (structural maintenance of chromosomes) complexes share conserved architectures and function in chromosome maintenance via an unknown mechanism. Here we have used single-molecule techniques to study MukBEF, the SMC complex in Escherichia coli. Real-time movies show MukB alone can compact DNA and...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Elsevier
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234588/ https://www.ncbi.nlm.nih.gov/pubmed/35770038 http://dx.doi.org/10.1016/j.bbrep.2022.101297 |
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author | Zhou, Man |
author_facet | Zhou, Man |
author_sort | Zhou, Man |
collection | PubMed |
description | SMC (structural maintenance of chromosomes) complexes share conserved architectures and function in chromosome maintenance via an unknown mechanism. Here we have used single-molecule techniques to study MukBEF, the SMC complex in Escherichia coli. Real-time movies show MukB alone can compact DNA and ATP inhibits DNA compaction by MukB. We observed that DNA unidirectionally slides through MukB, potentially by a ratchet mechanism, and the sliding speed depends on the elastic energy stored in the DNA. MukE, MukF and ATP binding stabilize MukB and DNA interaction, and ATP hydrolysis regulates the loading/unloading of MukBEF from DNA. Our data suggests a new model for how MukBEF organizes the bacterial chromosome in vivo; and this model will be relevant for other SMC proteins. |
format | Online Article Text |
id | pubmed-9234588 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-92345882022-06-28 DNA sliding and loop formation by E. coli SMC complex: MukBEF Zhou, Man Biochem Biophys Rep Research Article SMC (structural maintenance of chromosomes) complexes share conserved architectures and function in chromosome maintenance via an unknown mechanism. Here we have used single-molecule techniques to study MukBEF, the SMC complex in Escherichia coli. Real-time movies show MukB alone can compact DNA and ATP inhibits DNA compaction by MukB. We observed that DNA unidirectionally slides through MukB, potentially by a ratchet mechanism, and the sliding speed depends on the elastic energy stored in the DNA. MukE, MukF and ATP binding stabilize MukB and DNA interaction, and ATP hydrolysis regulates the loading/unloading of MukBEF from DNA. Our data suggests a new model for how MukBEF organizes the bacterial chromosome in vivo; and this model will be relevant for other SMC proteins. Elsevier 2022-06-22 /pmc/articles/PMC9234588/ /pubmed/35770038 http://dx.doi.org/10.1016/j.bbrep.2022.101297 Text en Crown Copyright © 2022 Published by Elsevier B.V. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Article Zhou, Man DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title | DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title_full | DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title_fullStr | DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title_full_unstemmed | DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title_short | DNA sliding and loop formation by E. coli SMC complex: MukBEF |
title_sort | dna sliding and loop formation by e. coli smc complex: mukbef |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234588/ https://www.ncbi.nlm.nih.gov/pubmed/35770038 http://dx.doi.org/10.1016/j.bbrep.2022.101297 |
work_keys_str_mv | AT zhouman dnaslidingandloopformationbyecolismccomplexmukbef |