The Molecular Basis for the Control of Cell Division

1976 ◽  
pp. 240-248 ◽  
Author(s):  
R. J. Inglis ◽  
H. R. Matthews ◽  
E. M. Bradbury
Keyword(s):  
Cell Division ◽  
Molecular Basis

scholarly journals c-di-GMP heterogeneity is generated by the chemotaxis machinery to regulate flagellar motility

eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Bridget R Kulasekara ◽  
Cassandra Kamischke ◽  
Hemantha D Kulasekara ◽  
Matthias Christen ◽  
Paul A Wiggins ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Division ◽  
Histidine Kinase ◽  
Molecular Basis ◽  
Individual Cell ◽  
Cell Heterogeneity ◽  
Flagellar Motility ◽  
Bacterial Populations ◽  
Phosphorylation State ◽  
Asymmetric Partitioning

Individual cell heterogeneity is commonly observed within populations, although its molecular basis is largely unknown. Previously, using FRET-based microscopy, we observed heterogeneity in cellular c-di-GMP levels. In this study, we show that c-di-GMP heterogeneity in Pseudomonas aeruginosa is promoted by a specific phosphodiesterase partitioned after cell division. We found that subcellular localization and reduction of c-di-GMP levels by this phosphodiesterase is dependent on the histidine kinase component of the chemotaxis machinery, CheA, and its phosphorylation state. Therefore, individual cell heterogeneity in c-di-GMP concentrations is regulated by the activity and the asymmetrical inheritance of the chemotaxis organelle after cell division. c-di-GMP heterogeneity results in a diversity of motility behaviors. The generation of diverse intracellular concentrations of c-di-GMP by asymmetric partitioning is likely important to the success and survival of bacterial populations within the environment by allowing a variety of motility behaviors.

Molecular basis of control of mitotic cell division in eukaryotes

Nature ◽  
1974 ◽  
Vol 249 (5457) ◽  
pp. 553-556 ◽  
Author(s):  
E. M. BRADBURY ◽  
R. J. INGLIS ◽  
H. R. MATTHEWS ◽  
T. A. LANGAN
Keyword(s):  
Cell Division ◽  
Molecular Basis ◽  
Mitotic Cell ◽  
Mitotic Cell Division

scholarly journals The C-terminal helix of BubR1 is essential for CENP-E-dependent chromosome alignment

2020 ◽  
Author(s):  
Thibault Legal ◽  
Daniel Hayward ◽  
Agata Gluszek-Kustusz ◽  
Elizabeth A. Blackburn ◽  
Christos Spanos ◽  
...  
Keyword(s):  
Cell Division ◽  
Molecular Basis ◽  
Spindle Checkpoint ◽  
Checkpoint Protein ◽  
Molecular Determinants ◽  
Chromosome Alignment

AbstractDuring cell division, misaligned chromosomes are captured and aligned by motors before their segregation. The CENP-E motor is recruited to polar unattached kinetochores, to facilitate chromosome alignment. The spindle checkpoint protein BubR1 has been reported as a CENP-E interacting partner, but to what extent, if at all, BubR1 contributes to CENP-E localization at kinetochores, has remained controversial. Here we define the molecular determinants that specify the interaction between BubR1 and CENP-E. The basic C-terminal helix of BubR1 is necessary but not sufficient for CENP-E interaction, while a minimal key acidic patch on the kinetochore-targeting domain of CENP-E, is also essential. We then demonstrate that BubR1 is required for the recruitment of CENP-E to kinetochores to facilitate chromosome alignment. This BubR1-CENP-E axis is critical to align chromosomes that have failed to congress through other pathways and recapitulates the major known function of CENP-E. Overall, our studies define the molecular basis and the function for CENP-E recruitment to BubR1 at kinetochores during mammalian mitosis.

scholarly journals Towards understanding the molecular basis of bacterial DNA segregation

2005 ◽  
Vol 360 (1455) ◽  
pp. 523-535 ◽  
Author(s):  
Thomas A Leonard ◽  
Jakob Møller-Jensen ◽  
Jan Löwe
Keyword(s):  
Cell Division ◽  
Chromosome Segregation ◽  
Plasmid Dna ◽  
Molecular Basis ◽  
Coordinated Control ◽  
Rapid Separation ◽  
Bacterial Dna ◽  
Dna Segregation ◽  
Dna Partitioning ◽  
And Control

Bacteria ensure the fidelity of genetic inheritance by the coordinated control of chromosome segregation and cell division. Here, we review the molecules and mechanisms that govern the correct subcellular positioning and rapid separation of newly replicated chromosomes and plasmids towards the cell poles and, significantly, the emergence of mitotic-like machineries capable of segregating plasmid DNA. We further describe surprising similarities between proteins involved in DNA partitioning (ParA/ParB) and control of cell division (MinD/MinE), suggesting a mechanism for intracellular positioning common to the two processes. Finally, we discuss the role that the bacterial cytoskeleton plays in DNA partitioning and the missing link between prokaryotes and eukaryotes that is bacterial mechano-chemical motor proteins.

scholarly journals The chromosomal passenger complex controls the function of endosomal sorting complex required for transport-III Snf7 proteins during cytokinesis

Open Biology ◽  
2012 ◽  
Vol 2 (5) ◽  
pp. 120070 ◽  
Author(s):  
Luisa Capalbo ◽  
Emilie Montembault ◽  
Tetsuya Takeda ◽  
Zuni I. Bassi ◽  
David M. Glover ◽  
...  
Keyword(s):  
Cell Division ◽  
Molecular Basis ◽  
Cleavage Site ◽  
Human Cells ◽  
Membrane Association ◽  
Aurora B ◽  
Chromosomal Passenger Complex ◽  
Endosomal Sorting ◽  
Daughter Cells ◽  
Chromosomal Passenger

Summary Cytokinesis controls the proper segregation of nuclear and cytoplasmic materials at the end of cell division. The chromosomal passenger complex (CPC) has been proposed to monitor the final separation of the two daughter cells at the end of cytokinesis in order to prevent cell abscission in the presence of DNA at the cleavage site, but the precise molecular basis for this is unclear. Recent studies indicate that abscission could be mediated by the assembly of filaments comprising components of the endosomal sorting complex required for transport-III (ESCRT-III). Here, we show that the CPC subunit Borealin interacts directly with the Snf7 components of ESCRT-III in both Drosophila and human cells. Moreover, we find that the CPC's catalytic subunit, Aurora B kinase, phosphorylates one of the three human Snf7 paralogues—CHMP4C—in its C-terminal tail, a region known to regulate its ability to form polymers and associate with membranes. Phosphorylation at these sites appears essential for CHMP4C function because their mutation leads to cytokinesis defects. We propose that CPC controls abscission timing through inhibition of ESCRT-III Snf7 polymerization and membrane association using two concurrent mechanisms: interaction of its Borealin component with Snf7 proteins and phosphorylation of CHMP4C by Aurora B.

scholarly journals Structural evidence for Scc4-dependent localization of cohesin loading

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Stephen M Hinshaw ◽  
Vasso Makrantoni ◽  
Alastair Kerr ◽  
Adèle L Marston ◽  
Stephen C Harrison
Keyword(s):  
Crystal Structure ◽  
Transcriptional Regulation ◽  
Cell Division ◽  
Molecular Basis ◽  
Developmental Defects ◽  
Chromosome Missegregation ◽  
Sister Chromatids ◽  
Chromatid Cohesion ◽  
Multicellular Organisms

The cohesin ring holds newly replicated sister chromatids together until their separation at anaphase. Initiation of sister chromatid cohesion depends on a separate complex, Scc2NIPBL/Scc4Mau2 (Scc2/4), which loads cohesin onto DNA and determines its localization across the genome. Proper cohesin loading is essential for cell division, and partial defects cause chromosome missegregation and aberrant transcriptional regulation, leading to severe developmental defects in multicellular organisms. We present here a crystal structure showing the interaction between Scc2 and Scc4. Scc4 is a TPR array that envelops an extended Scc2 peptide. Using budding yeast, we demonstrate that a conserved patch on the surface of Scc4 is required to recruit Scc2/4 to centromeres and to build pericentromeric cohesion. These findings reveal the role of Scc4 in determining the localization of cohesin loading and establish a molecular basis for Scc2/4 recruitment to centromeres.

scholarly journals The C-terminal helix of BubR1 is essential for CENP-E-dependent chromosome alignment

2020 ◽  
Vol 133 (16) ◽  
pp. jcs246025 ◽  
Author(s):  
Thibault Legal ◽  
Daniel Hayward ◽  
Agata Gluszek-Kustusz ◽  
Elizabeth A. Blackburn ◽  
Christos Spanos ◽  
...  
Keyword(s):  
Cell Division ◽  
Molecular Basis ◽  
Spindle Checkpoint ◽  
First Person ◽  
Checkpoint Protein ◽  
Molecular Determinants ◽  
Chromosome Alignment

ABSTRACTDuring cell division, misaligned chromosomes are captured and aligned by motors before their segregation. The CENP-E motor is recruited to polar unattached kinetochores to facilitate chromosome alignment. The spindle checkpoint protein BubR1 (also known as BUB1B) has been reported as a CENP-E interacting partner, but the extent to which BubR1 contributes to CENP-E localization at kinetochores has remained controversial. Here we define the molecular determinants that specify the interaction between BubR1 and CENP-E. The basic C-terminal helix of BubR1 is necessary but not sufficient for CENP-E interaction, and a minimal key acidic patch on the kinetochore-targeting domain of CENP-E is also essential. We then demonstrate that BubR1 is required for the recruitment of CENP-E to kinetochores to facilitate chromosome alignment. This BubR1–CENP-E axis is critical for alignment of chromosomes that have failed to congress through other pathways and recapitulates the major known function of CENP-E. Overall, our studies define the molecular basis and the function for CENP-E recruitment to BubR1 at kinetochores during mammalian mitosis.This article has an associated First Person interview with the first author of the paper.

scholarly journals Membrane fission during bacterial spore development requires DNA-driven cellular inflation

2021 ◽  
Author(s):  
Ane Landajuela ◽  
Martha Braun ◽  
Alejandro Martinez-Calvo ◽  
Christopher D. A. Rodrigues ◽  
Thierry Doan ◽  
...  
Keyword(s):  
Cell Division ◽  
Mother Cell ◽  
Complete Genome ◽  
Molecular Basis ◽  
Membrane Tension ◽  
Dna Translocation ◽  
Cell Cytoplasm ◽  
Membrane Fission ◽  
Catalyzed Membrane ◽  
Dna Translocase

Bacteria require membrane fission for cell division and endospore formation. FisB catalyzes membrane fission during sporulation, but the molecular basis is unclear as it cannot remodel membranes by itself. Sporulation initiates with an asymmetric division that generates a large mother cell and a smaller forespore that contains only 1/4 of its complete genome. As the mother cell membranes engulf the forespore, a DNA translocase pumps the rest of the chromosome into the small forespore compartment, inflating it due to increased turgor. When the engulfing membranes undergo fission, the forespore is released into the mother cell cytoplasm. Here we show that forespore inflation and FisB accumulation are both required for efficient membrane fission. We suggest that high membrane tension in the engulfment membrane caused by forespore inflation drives FisB-catalyzed membrane fission. Collectively our data indicate that DNA-translocation has a previously unappreciated second function in energizing FisB-mediated membrane fission under energy-limited conditions.

scholarly journals The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Sandeep K Talapatra ◽  
Bethany Harker ◽  
Julie PI Welburn
Keyword(s):  
Cell Division ◽  
Conformational Changes ◽  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Motor Protein ◽  
Atpase Domain ◽  
Conformational Switch ◽  
C Terminus ◽  
Structure And Activity ◽  
Motor Interaction

The precise regulation of microtubule dynamics is essential during cell division. The kinesin-13 motor protein MCAK is a potent microtubule depolymerase. The divergent non-motor regions flanking the ATPase domain are critical in regulating its targeting and activity. However, the molecular basis for the function of the non-motor regions within the context of full-length MCAK is unknown. Here, we determine the structure of MCAK motor domain bound to its regulatory C-terminus. Our analysis reveals that the MCAK C-terminus binds to two motor domains in solution and is displaced allosterically upon microtubule binding, which allows its robust accumulation at microtubule ends. These results demonstrate that MCAK undergoes long-range conformational changes involving its C-terminus during the soluble to microtubule-bound transition and that the C-terminus-motor interaction represents a structural intermediate in the MCAK catalytic cycle. Together, our work reveals intrinsic molecular mechanisms underlying the regulation of kinesin-13 activity.

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