The ParB clamp docks onto Smc for DNA loading via a joint-ParB interface

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

doi:10.1101/2021.12.15.472096

Cited by 3 publications

(4 citation statements)

References 63 publications

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“…Our analysis suggests the species-specific tuning of ParB—ParA interactions. Recently similar significance of species dependent interactions between ParB and SMC was reported ( Bock et al, 2021 ).…”

Section: Discussionsupporting

confidence: 71%

Genus-Specific Interactions of Bacterial Chromosome Segregation Machinery Are Critical for Their Function

et al. 2022

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Most bacteria use the ParABS system to segregate their newly replicated chromosomes. The two protein components of this system from various bacterial species share their biochemical properties: ParB is a CTPase that binds specific centromere-like parS sequences to assemble a nucleoprotein complex, while the ParA ATPase forms a dimer that binds DNA non-specifically and interacts with ParB complexes. The ParA-ParB interaction incites the movement of ParB complexes toward the opposite cell poles. However, apart from their function in chromosome segregation, both ParAB may engage in genus-specific interactions with other protein partners. One such example is the polar-growth controlling protein DivIVA in Actinomycetota, which binds ParA in Mycobacteria while interacts with ParB in Corynebacteria. Here, we used heterologous hosts to investigate whether the interactions between DivIVA and ParA or ParB are maintained across phylogenic classes. Specifically, we examined interactions of proteins from four bacterial species, two belonging to the Gram positive Actinomycetota phylum and two belonging to the Gram-negative Pseudomonadota. We show that while the interactions between ParA and ParB are preserved for closely related orthologs, the interactions with polarly localised protein partners are not conferred by orthologous ParABs. Moreover, we demonstrate that heterologous ParA cannot substitute for endogenous ParA, despite their high sequence similarity. Therefore, we conclude that ParA orthologs are fine-tuned to interact with their partners, especially their interactions with polarly localised proteins are adjusted to particular bacterial species demands.

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Section: Discussionsupporting

confidence: 71%

Genus-Specific Interactions of Bacterial Chromosome Segregation Machinery Are Critical for Their Function

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 (Böhm et al, 2020;Gruber and Errington, 2009;Minnen et al, 2011;Sullivan et al, 2009). It has recently been proposed in that loading results from a direct interaction between the SMC joint and the N-terminal CTP-binding domain of Spo0J (Bock et al, 2021). 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 (Wang et al, 2017;Wang et al, 2015).…”

Section: Involvement Of Smc/condensin In Axial Filament Formation and Its Regulation By Soj/paramentioning

confidence: 85%

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

Roberts

Anchimiuk

Kloosterman

et al. 2021

Preprint

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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 ATP-dependent dimerization and DNA binding, leading to chromosome segregation and SMC loading. 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. We now show that a major redistribution of SMC complexes drives axial filament formation, in a process regulated by ParA/Soj. Unexpectedly, this regulation is dependent on monomeric forms of ParA/Soj that cannot bind DNA or hydrolyse ATP. These results reveal a new role 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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“…In other bacteria, ParB recruits structural maintenance of the chromosome (SMC) complexes to the oriC region [61][62][63] . 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 [61][62][63][64][65][66][67] . 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 63 (Extended Data Fig.…”

Section: Parb Recruits Smc To the Chromosomal Replication Originsmentioning

confidence: 99%

“…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 [61][62][63] . 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 [61][62][63][64][65][66][67] .…”

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

Takacs

Wachter

Xiang

et al. 2022

Preprint

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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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The ParB clamp docks onto Smc for DNA loading via a joint-ParB interface

Cited by 3 publications

References 63 publications

Genus-Specific Interactions of Bacterial Chromosome Segregation Machinery Are Critical for Their Function

Genus-Specific Interactions of Bacterial Chromosome Segregation Machinery Are Critical for Their Function

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

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

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