Competitive binding of MatP and topoisomerase IV to the MukB hinge domain

Structural Maintenance of Chromosomes (SMC) complexes have ubiquitous roles in compacting DNA linearly, thereby promoting chromosome organization-segregation. Interaction between the Escherichia coli SMC complex, MukBEF, and matS-bound MatP in the chromosome replication termination region, ter, resu...

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Autores principales:	Gemma LM Fisher, Jani R Bolla, Karthik V Rajasekar, Jarno Mäkelä, Rachel Baker, Man Zhou, Josh P Prince, Mathew Stracy, Carol V Robinson, Lidia K Arciszewska, David J Sherratt
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	chromosome SMC MukBEF MatP topoisomerase IV Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e79ddc8ecbd14d45bbe14bac256ab85d
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spelling	oai:doaj.org-article:e79ddc8ecbd14d45bbe14bac256ab85d2021-12-01T10:57:11ZCompetitive binding of MatP and topoisomerase IV to the MukB hinge domain10.7554/eLife.704442050-084Xe70444https://doaj.org/article/e79ddc8ecbd14d45bbe14bac256ab85d2021-09-01T00:00:00Zhttps://elifesciences.org/articles/70444https://doaj.org/toc/2050-084XStructural Maintenance of Chromosomes (SMC) complexes have ubiquitous roles in compacting DNA linearly, thereby promoting chromosome organization-segregation. Interaction between the Escherichia coli SMC complex, MukBEF, and matS-bound MatP in the chromosome replication termination region, ter, results in depletion of MukBEF from ter, a process essential for efficient daughter chromosome individualization and for preferential association of MukBEF with the replication origin region. Chromosome-associated MukBEF complexes also interact with topoisomerase IV (ParC2E2), so that their chromosome distribution mirrors that of MukBEF. We demonstrate that MatP and ParC have an overlapping binding interface on the MukB hinge, leading to their mutually exclusive binding, which occurs with the same dimer to dimer stoichiometry. Furthermore, we show that matS DNA competes with the MukB hinge for MatP binding. Cells expressing MukBEF complexes that are mutated at the ParC/MatP binding interface are impaired in ParC binding and have a mild defect in MukBEF function. These data highlight competitive binding as a means of globally regulating MukBEF-topoisomerase IV activity in space and time.Gemma LM FisherJani R BollaKarthik V RajasekarJarno MäkeläRachel BakerMan ZhouJosh P PrinceMathew StracyCarol V RobinsonLidia K ArciszewskaDavid J SherratteLife Sciences Publications LtdarticlechromosomeSMCMukBEFMatPtopoisomerase IVMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	chromosome SMC MukBEF MatP topoisomerase IV Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	chromosome SMC MukBEF MatP topoisomerase IV Medicine R Science Q Biology (General) QH301-705.5 Gemma LM Fisher Jani R Bolla Karthik V Rajasekar Jarno Mäkelä Rachel Baker Man Zhou Josh P Prince Mathew Stracy Carol V Robinson Lidia K Arciszewska David J Sherratt Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
description	Structural Maintenance of Chromosomes (SMC) complexes have ubiquitous roles in compacting DNA linearly, thereby promoting chromosome organization-segregation. Interaction between the Escherichia coli SMC complex, MukBEF, and matS-bound MatP in the chromosome replication termination region, ter, results in depletion of MukBEF from ter, a process essential for efficient daughter chromosome individualization and for preferential association of MukBEF with the replication origin region. Chromosome-associated MukBEF complexes also interact with topoisomerase IV (ParC2E2), so that their chromosome distribution mirrors that of MukBEF. We demonstrate that MatP and ParC have an overlapping binding interface on the MukB hinge, leading to their mutually exclusive binding, which occurs with the same dimer to dimer stoichiometry. Furthermore, we show that matS DNA competes with the MukB hinge for MatP binding. Cells expressing MukBEF complexes that are mutated at the ParC/MatP binding interface are impaired in ParC binding and have a mild defect in MukBEF function. These data highlight competitive binding as a means of globally regulating MukBEF-topoisomerase IV activity in space and time.
format	article
author	Gemma LM Fisher Jani R Bolla Karthik V Rajasekar Jarno Mäkelä Rachel Baker Man Zhou Josh P Prince Mathew Stracy Carol V Robinson Lidia K Arciszewska David J Sherratt
author_facet	Gemma LM Fisher Jani R Bolla Karthik V Rajasekar Jarno Mäkelä Rachel Baker Man Zhou Josh P Prince Mathew Stracy Carol V Robinson Lidia K Arciszewska David J Sherratt
author_sort	Gemma LM Fisher
title	Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
title_short	Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
title_full	Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
title_fullStr	Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
title_full_unstemmed	Competitive binding of MatP and topoisomerase IV to the MukB hinge domain
title_sort	competitive binding of matp and topoisomerase iv to the mukb hinge domain
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/e79ddc8ecbd14d45bbe14bac256ab85d
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Competitive binding of MatP and topoisomerase IV to the MukB hinge domain

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