A joint-ParB interface promotes Smc DNA recruitment

Bock, Florian Patrick; Liu, Hon Wing; Anchimiuk, Anna; Diebold-Durand, Marie-Laure; Gruber, Stephan

doi:10.1016/j.celrep.2022.111273

Cited by 17 publications

(14 citation statements)

References 61 publications

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“…Therefore, we investigated whether ParB achieves this function via interaction with another protein. In other bacteria, ParB recruits structural maintenance of the chromosome (SMC) complexes to the oriC region [64][65][66] . The recruitment of SMC to oriC and subsequent organization of the oriC region have been shown to facilitate oriC segregation in Caulobacter crescentus and Bacillus subtilis [64][65][66][67][68][69][70] .…”

Section: Parb Recruits Smc To the Chromosomal Replication Originsmentioning

confidence: 99%

“…In other bacteria, ParB recruits structural maintenance of the chromosome (SMC) complexes to the oriC region [64][65][66] . The recruitment of SMC to oriC and subsequent organization of the oriC region have been shown to facilitate oriC segregation in Caulobacter crescentus and Bacillus subtilis [64][65][66][67][68][69][70] . While lacking the ParA control motif, the B. burgdorferi ParB protein has retained a predicted SMC-binding region located within the N-terminal domain of ParB 66 (Supplementary Fig.…”

Section: Parb Recruits Smc To the Chromosomal Replication Originsmentioning

confidence: 99%

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Polyploidy, regular patterning of genome copies, and unusual control of DNA partitioning in the Lyme disease spirochete

et al. 2022

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Borrelia burgdorferi, the tick-transmitted spirochete agent of Lyme disease, has a highly segmented genome with a linear chromosome and various linear or circular plasmids. Here, by imaging several chromosomal loci and 16 distinct plasmids, we show that B. burgdorferi is polyploid during growth in culture and that the number of genome copies decreases during stationary phase. B. burgdorferi is also polyploid inside fed ticks and chromosome copies are regularly spaced along the spirochete’s length in both growing cultures and ticks. This patterning involves the conserved DNA partitioning protein ParA whose localization is controlled by a potentially phage-derived protein, ParZ, instead of its usual partner ParB. ParZ binds its own coding region and acts as a centromere-binding protein. While ParA works with ParZ, ParB controls the localization of the condensin, SMC. Together, the ParA/ParZ and ParB/SMC pairs ensure faithful chromosome inheritance. Our findings underscore the plasticity of cellular functions, even those as fundamental as chromosome segregation.

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Section: Parb Recruits Smc To the Chromosomal Replication Originsmentioning

confidence: 99%

Section: Parb Recruits Smc To the Chromosomal Replication Originsmentioning

confidence: 99%

Polyploidy, regular patterning of genome copies, and unusual control of DNA partitioning in the Lyme disease spirochete

et al. 2022

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“…It is well established that SMC complexes are loaded onto the chromosome at the origin region by Spo0J bound around parS sites in many bacterial species (3,15,34,41,42). It has recently been proposed that loading results from a direct interaction between the SMC joint and the N-terminal CTPbinding domain of Spo0J (84). At some point, SMC complexes will become released from the loading site and translocate along the chromosome to facilitate chromosome segregation and organization, as previously mentioned (37,39).…”

Section: Apo-and Atp-bound Monomers Of Soj Have Differentiatedmentioning

confidence: 87%

Chromosome remodelling by SMC/Condensin in B. subtilis is regulated by monomeric Soj/ParA during growth and sporulation

Roberts

Anchimiuk

Kloosterman

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

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SMC complexes, loaded at ParB- parS sites, are key mediators of chromosome organization in bacteria. ParA/Soj proteins interact with ParB/Spo0J in a pathway involving adenosine triphosphate (ATP)-dependent dimerization and DNA binding, facilitating chromosome segregation in bacteria. In Bacillus subtilis , ParA/Soj also regulates DNA replication initiation and along with ParB/Spo0J is involved in cell cycle changes during endospore formation. The first morphological stage in sporulation is the formation of an elongated chromosome structure called an axial filament. Here, we show that a major redistribution of SMC complexes drives axial filament formation in a process regulated by ParA/Soj. Furthermore, and unexpectedly, this regulation is dependent on monomeric forms of ParA/Soj that cannot bind DNA or hydrolyze ATP. These results reveal additional roles for ParA/Soj proteins in the regulation of SMC dynamics in bacteria and yet further complexity in the web of interactions involving chromosome replication, segregation and organization, controlled by ParAB and SMC.

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“…The hairpins and helices of the structured regime may facilitate the loading of SMC (structural maintenance of chromosomes) complexes onto the DNA (41). While this is known to be due to ParB at the parS sites (42), the precise mechanism is a topic of ongoing study (43, 44). However, ParB mutations that eliminate SMC recruitment are also known to reduce the ability of ParB to form a higher-order nucleoprotein complex (43, 45, 46).…”

Section: Discussionmentioning

confidence: 99%

Partition complex structure can arise from sliding and bridging of ParB dimers

Connolley¹,

Schnabel²,

Thanbichler³

et al. 2022

Preprint

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Chromosome segregation is vital for cell replication and in many bacteria is controlled by the ParABS system. A key part of this machinery is the association of ParB proteins to the parS-containing centromeric region to form the partition complex. Despite much work, the formation and structure of this nucleoprotein complex has remained unclear. However, it was recently discovered that CTP binding allows ParB dimers to entrap and slide along the DNA, as well as leading to more efficient condensation through ParB-mediated DNA bridging. Here, we use semi-flexible polymer simulations to show how these properties of sliding and bridging can explain partition complex formation. We find that transient ParB bridges can organise the DNA into either a globular state or into hairpins and helical structures, depending on the bridge lifetime. In separate stochastic simulations, we show that ParB sliding reproduces the experimentally measured multi-peaked binding profile of Caulobacter crescentus, indicating that bridging and other potential roadblocks are sufficiently short-lived that they do not hinder ParB spreading. Indeed, upon coupling the two simulation frameworks into a unified sliding and bridging model, we find that short-lived ParB bridges do not hinder ParB sliding and the model can reproduce both the ParB binding profile and the condensation of the nucleoprotein complex. Overall, our model clarifies the mechanism of partition complex formation and predicts its fine structure. We speculate that the DNA hairpins produced by ParB bridging underlie the secondary function of ParB to load the Structural Maintenance of Chromosome (SMC) complex onto the DNA.

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A joint-ParB interface promotes Smc DNA recruitment

Cited by 17 publications

References 61 publications

Polyploidy, regular patterning of genome copies, and unusual control of DNA partitioning in the Lyme disease spirochete

Polyploidy, regular patterning of genome copies, and unusual control of DNA partitioning in the Lyme disease spirochete

Chromosome remodelling by SMC/Condensin in B. subtilis is regulated by monomeric Soj/ParA during growth and sporulation

Partition complex structure can arise from sliding and bridging of ParB dimers

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