Mechanisms for Chromosome Segregation in Bacteria

Gogou, Christos; Japaridze, Aleksandre; Dekker, Cees

doi:10.3389/fmicb.2021.685687

Cited by 38 publications

(42 citation statements)

References 173 publications

(266 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…So, there are multiple observations that exemplify MatP’s involvement in the tight regulation of TopoIV-mediated sister-resolution at ter: MatP’s competition with TopoIV to bind MukB 19 , its function to actively displace MukBEF from ter, and the XerCD-TopoIV interaction. XerCD necessitates and specifically guides TopoIV to dif to resolve concatenated sisters 54 . matP deletion can therefore disrupt chromosome recombination, leading to a single toroidal dimer chromosome instead of properly decatenated sisters.…”

Section: Discussionmentioning

confidence: 99%

MukBEF-dependent chromosomal organization in widened Escherichia coli

Japaridze

Wee

Gogou

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

The bacterial chromosome is spatially organized through protein-mediated compaction, supercoiling, and cell-boundary confinement. Structural Maintenance of Chromosomes (SMC) complexes are a major class of chromosome-organizing proteins present throughout all domains of life. Here, we study the role of the Escherichia coli SMC complex MukBEF in chromosome architecture and segregation. Using quantitative live-cell imaging of shape-manipulated cells, we show that MukBEF is crucial to preserve the toroidal topology of the E. coli chromosome and that it is non-uniformly distributed along the chromosome: it prefers locations towards the origin and away from the terminus of replication, and it is unevenly distributed over the origin of replication along the two chromosome arms. Using an ATP hydrolysis-deficient MukB mutant, we find that MukBEF translocation along the chromosome is ATP-dependent, in contrast to its loading onto DNA. MukBEF and MatP are furthermore found to be essential for sister chromosome decatenation. We propose a model that explains how MukBEF, MatP, and their interacting partners organize the chromosome and contribute to sister segregation and recombination. The combination of bacterial cell-shape modification and quantitative fluorescence microscopy paves way to investigating chromosome-organization factors in vivo.

show abstract

Section: Discussionmentioning

confidence: 99%

MukBEF-dependent chromosomal organization in widened Escherichia coli

Japaridze

Wee

Gogou

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…We assume that PPK1 AT is not a migrating protein per se but is able to bind to another protein or molecule that is moving during the cell cycle and, thus, could explain the movement of PPK1 AT and/or PPK1 AT with associated polyP. The genome of each cell must replicate and segregate during cell division (for recent reviews on DNA segregation systems see [Gogou et al, 2021;Hu et al, 2021]), and this process includes an active movement of the daughter chromosome(s) to the upcoming daughter cell. We, therefore, hypothesized that PPK1 AT could interact with and bind to DNA, thus explaining the observed movement shortly before cell division.…”

Section: Movement Of Polyp Granules In the Presence Of Mitomycin Cmentioning

confidence: 99%

Migration of Polyphosphate Granules in Agrobacterium tumefaciens

et al. 2022

View full text Add to dashboard Cite

Agrobacterium tumefaciens has two polyphosphate (polyP) kinases, one of which (PPK1AT) is responsible for the formation of polyP granules, while the other (PPK2AT) is used for replenishing the NTP pools by using polyP as a phosphate donor to phosphorylate nucleoside diphosphates. Fusions of eYFP with PPK2AT or of the polyP granule-associated phosin PptA from Ralstonia eutropha always co-localized with polyP granules in A. tumefaciens and allowed the tracking of polyP granules in time-lapse microscopy experiments without the necessity to label the cells with the toxic dye DAPI. Fusions of PPK1AT with mCherry formed fluorescent signals often attached to, but not completely co-localizing with, polyP granules in wild-type cells. Time-lapse microscopy revealed that polyP granules in about one-third of a cell population migrated from the old pole to the new cell pole shortly before or during cell division. Many cells de novo formed a second (nonmigrating) polyP granule at the opposite cell pole before cell division was completed, resulting in two daughter cells each having a polyP granule at the old pole after septum formation. Migration of polyP granules was disordered in mitomycin C-treated or in PopZ-depleted cells, suggesting that polyP granules can associate with DNA or with other molecules that are segregated during the cell cycle.

show abstract

“…Single-molecule techniques have shed light into how certain NAPs bind, bend, kink, coat or stiffen short DNA molecules [6][7][8][9][10][11][12]; on the contrary, we have little understanding of how they work in crowded and entangled environments [5]. For instance, while it is recognised that DNA segregation is highly impaired when NAPs are removed from the cell [13], the NAPmediated mechanisms through which this organisation is achieved remain to be determined. Here, we focus on one of the most abundant NAPs, the Integration Host Factor (IHF).…”

mentioning

confidence: 99%

Fluidification of entanglements by a DNA bending protein

Fosado¹,

Howard²,

Noy³

et al. 2022

Preprint

View full text Add to dashboard Cite

In spite of the nanoscale insights into how nucleoid associated proteins (NAPs) interact with DNA in vitro, their role in modulating the mesoscale viscoelasticity of entangled cellular environments is not understood. By combining microrheology and molecular dynamics simulation we find that IHF -an abundant NAP -lowers the viscosity of entangled λDNA 20-fold at physiological stoichiometries. In turn, we expect that IHF may reduce the effective viscosity of the nucleoid ∼200-fold, suggesting a key role of DNA organisation in vivo as a genomic fluidiser.

show abstract

Mechanisms for Chromosome Segregation in Bacteria

Cited by 38 publications

References 173 publications

MukBEF-dependent chromosomal organization in widened Escherichia coli

MukBEF-dependent chromosomal organization in widened Escherichia coli

Migration of Polyphosphate Granules in <b><i>Agrobacterium tumefaciens</i></b>

Fluidification of entanglements by a DNA bending protein

Contact Info

Product

Resources

About