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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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Autor principal: Zhou, Man
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
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.
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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
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