Division Rings
Mostrando 13-24 de 51 artigos, teses e dissertações.
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13. Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
Dynamins are a eukaryote-specific family of GTPases. Some family members are involved in diverse and varied cellular activities. Here, we report that the primitive red alga Cyanidioschyzon merolae retains only one dynamin homolog, CmDnm1, belonging to the mitochondrial division subfamily. Previously, the bacterial cell division protein, FtsZ, was shown to lo
The National Academy of Sciences.
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14. Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated.
FtsZ is an essential division protein in bacteria that functions by forming a ring at midcell that mediates septation. To further study the function of the Z ring the effect of a temperature-sensitive mutation, ftsZ84(Ts), on ring dynamics and septal progression was examined. Shifting a strain carrying an ftsZ84(Ts) mutation to the nonpermissive temperature
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15. Only the N-Terminal Domain of FtsK Functions in Cell Division
Deletion of ftsK results in the inhibition of cell division, but this inhibition can be reversed by a plasmid carrying only the first ∼17% of ftsK. The division block can be suppressed in most mutants by deletion of dacA, which codes for the d-alanine:d-alanine carboxypeptidase PBP5, or in all mutants by overexpression of ftsN. Overexpression of ftsK inhib
American Society for Microbiology.
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16. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.
The bacterial cell division protein FtsZ is a homolog of tubulin, but it has not been determined whether FtsZ polymers are structurally related to the microtubule lattice. In the present study, we have obtained high-resolution electron micrographs of two FtsZ polymers that show remarkable similarity to tubulin polymers. The first is a two-dimensional sheet o
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17. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
ZipA and FtsA are recruited independently to the FtsZ cytokinetic ring (Z ring) and are essential for cell division of Escherichia coli. The molecular role of FtsA in cell division is unknown; however, ZipA is thought to stabilize the Z ring, anchor it to the membrane, and recruit downstream cell division proteins. Here we demonstrate that the requirement fo
The National Academy of Sciences.
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18. FtsZ Dynamics during the Division Cycle of Live Escherichia coli Cells
The dynamics and assembly of bacterial cell division protein FtsZ were monitored in individual, growing and dividing Escherichia coli cells in real time by microculture of a merodiploid strain expressing green fluorescent protein (GFP)-tagged FtsZ. Cells expressing FtsZ-GFP at levels less than or equivalent to that of wild-type FtsZ were able to grow and div
American Society for Microbiology.
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19. Novel Filaments 5 nm in Diameter Constitute the Cytosolic Ring of the Plastid Division Apparatus
The plastid division apparatus (called the plastid-dividing ring) has been detected in several plant and algal species at the constricted region of plastids by transmission electron microscopy. The apparatus is composed of two or three rings: an outer ring in the cytosol, an inner ring in the stroma, and a middle ring in the intermembrane space. The componen
American Society of Plant Physiologists.
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20. Z-Ring-Independent Interaction between a Subdomain of FtsA and Late Septation Proteins as Revealed by a Polar Recruitment Assay
FtsA, a member of the ATPase superfamily that includes actin and bacterial actin homologs, is essential for cell division of Escherichia coli and is recruited to the Z ring. In turn, recruitment of later essential division proteins to the Z ring is dependent on FtsA. In a polar recruitment assay, we found that FtsA can recruit at least two late proteins, Fts
American Society for Microbiology.
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21. A Plant-Specific Dynamin-Related Protein Forms a Ring at the Chloroplast Division Site
Chloroplasts have retained the bacterial FtsZ for division, whereas mitochondria lack FtsZ except in some lower eukaryotes. Instead, mitochondrial division involves a dynamin-related protein, suggesting that chloroplasts retained the bacterial division system, whereas a dynamin-based system replaced the bacterial system in mitochondria during evolution. In t
American Society of Plant Biologists.
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22. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
Positioning of the Z ring at the midcell site in Escherichia coli is assured by the min system, which masks polar sites through topological regulation of MinC, an inhibitor of division. To study how MinC inhibits division, we have generated a MalE-MinC fusion that retains full biological activity. We find that MalE-MinC interacts with FtsZ and prevents polym
The National Academy of Sciences.
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23. ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli
The MinC division inhibitor is required for accurate placement of the septal ring at the middle of the Escherichia coli cell. The N-terminal domain of MinC (ZMinC) interferes with FtsZ assembly, while the C-terminal domain (DMinC) mediates both dimerization and complex formation with either MinD or DicB. Binding to either of these activators greatly enhances
American Society for Microbiology.
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24. Recruitment of ZipA to the Septal Ring of Escherichia coli Is Dependent on FtsZ and Independent of FtsA
Cell division in prokaryotes is mediated by the septal ring. In Escherichia coli, this organelle consists of several essential division proteins, including FtsZ, FtsA, and ZipA. To gain more insight into how the structure is assembled, we studied the interdependence of FtsZ, FtsA, and ZipA localization using both immunofluorescence and Gfp tagging techniques
American Society for Microbiology.