Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex

Author:

Zhao Yilin1,Guo Lijuan1,Hu Jiaojiao23,Ren Zhiyun145,Li Yanan1ORCID,Hu Meng1,Zhang Xia1,Bi Lulu1,Li Dan67,Ma Hanhui1ORCID,Liu Cong23,Sun Bo1ORCID

Affiliation:

1. School of Life Science and Technology, ShanghaiTech University , Shanghai  201210 , China

2. Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences , Shanghai  201210 , China

3. State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences , Shanghai  200032 , China

4. CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences , Shanghai  200031 , China

5. University of Chinese Academy of Sciences , Beijing  100049 , China

6. Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University , Shanghai  200240 , China

7. Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University , Shanghai  200240 , China

Abstract

Abstract The tripartite ParABS system mediates chromosome segregation in the majority of bacterial species. Typically, DNA-bound ParB proteins around the parS sites condense the chromosomal DNA into a higher-order multimeric nucleoprotein complex for the ParA-driven partition. Despite extensive studies, the molecular mechanism underlying the dynamic assembly of the partition complex remains unclear. Herein, we demonstrate that Bacillus subtilis ParB (Spo0J), through the multimerization of its N-terminal domain, forms phase-separated condensates along a single DNA molecule, leading to the concurrent organization of DNA into a compact structure. Specifically, in addition to the co-condensation of ParB dimers with DNA, the engagement of well-established ParB condensates with DNA allows for the compression of adjacent DNA and the looping of distant DNA. Notably, the presence of CTP promotes the formation of condensates by a low amount of ParB at parS sites, triggering two-step DNA condensation. Remarkably, parS-centered ParB-DNA co-condensate constitutes a robust nucleoprotein architecture capable of withstanding disruptive forces of tens of piconewton. Overall, our findings unveil diverse modes of DNA compaction enabled by phase-separated ParB and offer new insights into the dynamic assembly and maintenance of the bacterial partition complex.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Shanghai

Science and Technology Commission of Shanghai Municipality

Shanghai Pilot Program for Basic Research – Chinese Academy of Science, Shanghai Branch

CAS Project for Young Scientists in Basic Research

Publisher

Oxford University Press (OUP)

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