CTP-controlled liquid–liquid phase separation of ParB

Babl, Leon; Giacomelli, Giacomo; Ramm, Beatrice; Gelmroth, Ann-Kathrin; Bramkamp, Marc; Schwille, Petra

doi:10.1016/j.jmb.2021.167401

Cited by 41 publications

(46 citation statements)

References 60 publications

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“…ParB has been recently shown to undergo Liquid-liquid phase separation (LLPS), favoring condensate formation in the presence of CTP (Babl et al, 2022 ). Liquid-liquid phase separation is a thermodynamic process wherein a homogeneous mixture of two or more molecules de-mixes into distinct phases and thus helps compartmentalize membrane-less organelles (Hyman et al, 2014 ; Guilhas et al, 2020 ; Babl et al, 2022 ). In most eukaryotic subcellular structures, like germline P-bodies (Brangwynne et al, 2009 ), stress granules (Protter and Parker, 2016 ) etc., compartmentalization depends upon LLPS.…”

Section: The Sopabc or Parabs L...mentioning

confidence: 99%

“…Recently, ParB has also been shown to exist in two different phases, a gas phase and a liquid phase. Further, in a process similar to the LLPS in eukaryotic proteins, ParB from Corynebacterium glutamicum also forms spherical assemblies in the presence of crowding agents, is affected by alterations in ionic strength and is stabilized by potassium glutamate (Babl et al, 2022 ). The condensation of ParB is further favored by the presence of parS containing DNA and the motor protein ParA helps in the separation of these condensates ( Figure 2C ).…”

Section: The Sopabc or Parabs L...mentioning

confidence: 99%

“…The condensation of ParB is further favored by the presence of parS containing DNA and the motor protein ParA helps in the separation of these condensates ( Figure 2C ). Moreover, in the case of the ParA F K120Q mutant, the condensates merge and do not segregate suggesting that the ParB stimulated ATPase activity of ParA is required to separate these condensates (Guilhas et al, 2020 ; Babl et al, 2022 ).…”

Section: The Sopabc or Parabs L...mentioning

confidence: 99%

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Catching a Walker in the Act—DNA Partitioning by ParA Family of Proteins

Mishra

Srinivasan

2022

Front. Microbiol.

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Partitioning the replicated genetic material is a crucial process in the cell cycle program of any life form. In bacteria, many plasmids utilize cytoskeletal proteins that include ParM and TubZ, the ancestors of the eukaryotic actin and tubulin, respectively, to segregate the plasmids into the daughter cells. Another distinct class of cytoskeletal proteins, known as the Walker A type Cytoskeletal ATPases (WACA), is unique to Bacteria and Archaea. ParA, a WACA family protein, is involved in DNA partitioning and is more widespread. A centromere-like sequence parS, in the DNA is bound by ParB, an adaptor protein with CTPase activity to form the segregation complex. The ParA ATPase, interacts with the segregation complex and partitions the DNA into the daughter cells. Furthermore, the Walker A motif-containing ParA superfamily of proteins is associated with a diverse set of functions ranging from DNA segregation to cell division, cell polarity, chemotaxis cluster assembly, cellulose biosynthesis and carboxysome maintenance. Unifying principles underlying the varied range of cellular roles in which the ParA superfamily of proteins function are outlined. Here, we provide an overview of the recent findings on the structure and function of the ParB adaptor protein and review the current models and mechanisms by which the ParA family of proteins function in the partitioning of the replicated DNA into the newly born daughter cells.

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Section: The Sopabc or Parabs L...mentioning

confidence: 99%

Section: The Sopabc or Parabs L...mentioning

confidence: 99%

Section: The Sopabc or Parabs L...mentioning

confidence: 99%

See 1 more Smart Citation

Catching a Walker in the Act—DNA Partitioning by ParA Family of Proteins

Mishra

Srinivasan

2022

Front. Microbiol.

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“…The localized loading and spreading and the CTP-mediated switch generate a zone of high ParB density around the oriC region that helps to structure the DNA. In vitro experiments suggest that ParB subunits form liquid-liquid phase separated condensate that may assist the segregation process in vivo [ 15 ]. The ParB– parS nucleoprotein complex is required for efficient oriC segregation.…”

Section: Introductionmentioning

confidence: 99%

“…In their ATP-bound form, ParA dimers bind to DNA, not specifically. ATP hydrolysis is then triggered by ParB, releasing ParA from the DNA [ 15 ]. This interaction between ParA and ParB generates a diffusion ratchet-type segregation mechanism, in which ParB condensates follow the highest concentration of ParA [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Subcellular Dynamics of a Conserved Bacterial Polar Scaffold Protein

Giacomelli

Feddersen

Feng

et al. 2022

Genes

Self Cite

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In order to survive, bacterial cells rely on precise spatiotemporal organization and coordination of essential processes such as cell growth, chromosome segregation, and cell division. Given the general lack of organelles, most bacteria are forced to depend on alternative localization mechanisms, such as, for example, geometrical cues. DivIVA proteins are widely distributed in mainly Gram-positive bacteria and were shown to bind the membrane, typically in regions of strong negative curvature, such as the cell poles and division septa. Here, they have been shown to be involved in a multitude of processes: from apical cell growth and chromosome segregation in actinobacteria to sporulation and inhibition of division re-initiation in firmicutes. Structural analyses revealed that DivIVA proteins can form oligomeric assemblies that constitute a scaffold for recruitment of other proteins. However, it remained unclear whether interaction with partner proteins influences DivIVA dynamics. Using structured illumination microscopy (SIM), single-particle tracking (SPT) microscopy, and fluorescent recovery after photobleaching (FRAP) experiments, we show that DivIVA from Corynebacterium glutamicum is mobilized by its binding partner ParB. In contrast, we show that the interaction between Bacillus subtilis DivIVA and its partner protein MinJ reduces DivIVA mobility. Furthermore, we show that the loss of the rod-shape leads to an increase in DivIVA dynamics in both organisms. Taken together, our study reveals the modulation of the polar scaffold protein by protein interactors and cell morphology. We reason that this leads to a very simple, yet robust way for actinobacteria to maintain polar growth and their rod-shape. In B. subtilis, however, the DivIVA protein is tailored towards a more dynamic function that allows quick relocalization from poles to septa upon division.

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Biomolecular Condensates: From Bacterial Compartments to Incubator Spaces of Emergent Chemical Systems in Matter‐to‐Life Transitions

Schnorr,

Childers

2024

ChemSystemsChem

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At the earliest development of prebiotic chemistry, bacterial cells were primarily viewed as “bags of molecules.” This longstanding viewpoint shaped and biased early research about life’s origins, setting an initial target when considering the path from prebiotic chemistry to modern life. The two fields of systems chemistry and bacterial cell biology seem like oil and water, but each brings their own perspectives and methods to consider “what is life?”. Here, we review the most recent discoveries in bacterial cell biology, focusing on biomolecular condensates to consider how they may impact our thinking of matter‐to‐life transitions. The presence of condensate compartments in the bacterial domain of life strengthens the hypothesis that condensates play roles in coordinating chemical systems in life’s origins. Bacterial condensates have been shown to enhance enzymatic reactions, tune substrate specificity, and be responsive to environmental conditions and metabolites. Systems chemistry studies have further illuminated the unique chemical environment within condensates and strategies for logically tying chemical processes to the formation and dissolution of condensates. We consider the potential of biomolecular condensates to provide “incubator spaces” where new chemistries can develop and examine future challenges regarding the capability of condensates to yield emergent chemical systems capable of selection.

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CTP-controlled liquid–liquid phase separation of ParB

Cited by 41 publications

References 60 publications

Catching a Walker in the Act—DNA Partitioning by ParA Family of Proteins

Catching a Walker in the Act—DNA Partitioning by ParA Family of Proteins

Subcellular Dynamics of a Conserved Bacterial Polar Scaffold Protein

Biomolecular Condensates: From Bacterial Compartments to Incubator Spaces of Emergent Chemical Systems in Matter‐to‐Life Transitions

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