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

eLife

David J Sherratt¹  Lidia K Arciszewska¹  Josh P Prince¹  Karthik V Rajasekar¹  Mathew Stracy¹  Man Zhou¹  Jarno Mäkelä¹  Gemma LM Fisher¹  Rachel Baker¹  Carol V Robinson²  Jani R Bolla² 

[1] Department of Biochemistry, University of Oxford, Oxford, United Kingdom;Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, United Kingdom;The Kavli Institute for Nanoscience Discovery, Oxford, United Kingdom;

关键词: chromosome;    SMC;    MukBEF;    MatP;    topoisomerase IV;    E. coli;   

DOI  :  10.7554/eLife.70444

来源: eLife Sciences Publications, Ltd

【 摘 要 】

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.

【 授权许可】

CC BY