Difference between revisions of "PMID:21216997"

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{|  id="Y4d9cb650df7dc"  class=" tableEdit PMID_info_table" 
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'''Hale, CA, Shiomi, D, Liu, B, Bernhardt, TG, Margolin, W, Niki, H and de Boer, PA'''  (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers.''J. Bacteriol.'' '''193''':1393-404
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!align=left  |Abstract
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Assembly of the cell division apparatus in bacteria starts with formation of the Z ring on the cytoplasmic face of the membrane. This process involves the accumulation of FtsZ polymers at midcell and their interaction with several FtsZ-binding proteins that collectively organize the polymers into a membrane-associated ring-like configuration. Three such proteins, FtsA, ZipA, and ZapA, have previously been identified in Escherichia coli. FtsA and ZipA are essential membrane-associated division proteins that help connect FtsZ polymers with the inner membrane. ZapA is a cytoplasmic protein that is not required for the fission process per se but contributes to its efficiency, likely by promoting lateral interactions between FtsZ protofilaments. We report the identification of YcbW (ZapC) as a fourth FtsZ-binding component of the Z ring in E. coli. Binding of ZapC promotes lateral interactions between FtsZ polymers and suppresses FtsZ GTPase activity. This and additional evidence indicate that, like ZapA, ZapC is a nonessential Z-ring component that contributes to the efficiency of the division process by stabilizing the polymeric form of FtsZ.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21216997 PubMed]
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Online version:[http://dx.doi.org/10.1128/JB.01245-10 10.1128/JB.01245-10]
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!align=left  |Keywords
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==Main Points of the Paper ==
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*''zapC'' is determined to be another member of the septal ring
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*ZapC suppresses FtsZ GTPase activity
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== Materials and Methods Used ==
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{{LitMaterials}}
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==Phenotype Annotations==
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{{AnnotationTableHelp}}
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{|  id="C4d9cb650eaf01"  class=" tableEdit PMID_Phenotype_table" 
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!|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes
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''Escherichia coli''
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BL5
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''zapC-Slm260''
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longer cell length in late-logrithmic growth
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Morphology
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when grown to late log phase, this mutant appears slightly longer on average than those of the wild-type parent, TB28
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Microscopy
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''Escherichia coli''
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BL5
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del ''minCDE'' ''zapC-Slm260''
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longer cell length in late-logrithmic growth
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Morphology
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when grown to late log phase, this mutant appears slightly longer on average than those of the wild-type parent, TB43
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Microscopy
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''Escherichia coli''
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BL6
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del ''minCDE'' ''zapC-Slm260''
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increased length-to-septum ratio
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Morphology
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increased from 17 micrometers in TB43 to 55 micrometers in BL6
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Microscopy
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Table 3
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''Escherichia coli''
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BL6
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del ''minCDE'' ''zapC-Slm260''
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filamentous
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Morphology
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suppressed by ectopic expression of ''zapC''
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Microscopy
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Figure 2
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==Notes==
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==References==
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{{RefHelp}}
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<references/>
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[[Category:Protein Purification, FtsZ]][[Category:Protein Purification, ZapC]][[Category:GTPase Activity Assay]][[Category:Light Scattering Assay]][[Category:Microscopy, Electron]][[Category:Microscopy, Fluorescence]][[Category: Microscopy, Differential Interference Contrast (DIC)]][[Category:Microscopy, Immunofluorescence (IF)]][[Category:Western Blot Analysis]][[Category:Yeast 2-Hybrid (Y2H) Assay]][[Category:Chromatography, Gel Filtration]][[Category:Cosedimentation Assay]]
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[[Category:Publication]]
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[[Category:To Be Converted]]

Latest revision as of 12:09, 22 June 2011

Citation

Hale, CA, Shiomi, D, Liu, B, Bernhardt, TG, Margolin, W, Niki, H and de Boer, PA (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers.J. Bacteriol. 193:1393-404

Abstract

Assembly of the cell division apparatus in bacteria starts with formation of the Z ring on the cytoplasmic face of the membrane. This process involves the accumulation of FtsZ polymers at midcell and their interaction with several FtsZ-binding proteins that collectively organize the polymers into a membrane-associated ring-like configuration. Three such proteins, FtsA, ZipA, and ZapA, have previously been identified in Escherichia coli. FtsA and ZipA are essential membrane-associated division proteins that help connect FtsZ polymers with the inner membrane. ZapA is a cytoplasmic protein that is not required for the fission process per se but contributes to its efficiency, likely by promoting lateral interactions between FtsZ protofilaments. We report the identification of YcbW (ZapC) as a fourth FtsZ-binding component of the Z ring in E. coli. Binding of ZapC promotes lateral interactions between FtsZ polymers and suppresses FtsZ GTPase activity. This and additional evidence indicate that, like ZapA, ZapC is a nonessential Z-ring component that contributes to the efficiency of the division process by stabilizing the polymeric form of FtsZ.

Links

PubMed Online version:10.1128/JB.01245-10

Keywords


edit table

Main Points of the Paper

  • zapC is determined to be another member of the septal ring
  • ZapC suppresses FtsZ GTPase activity

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.
<protect>

Species Taxon ID Strain Gene (if known) OMP Phenotype Details Evidence Notes

Escherichia coli

BL5

zapC-Slm260

longer cell length in late-logrithmic growth

Morphology

when grown to late log phase, this mutant appears slightly longer on average than those of the wild-type parent, TB28

Microscopy

Escherichia coli

BL5

del minCDE zapC-Slm260

longer cell length in late-logrithmic growth

Morphology

when grown to late log phase, this mutant appears slightly longer on average than those of the wild-type parent, TB43

Microscopy

Escherichia coli

BL6

del minCDE zapC-Slm260

increased length-to-septum ratio

Morphology

increased from 17 micrometers in TB43 to 55 micrometers in BL6

Microscopy

Table 3

Escherichia coli

BL6

del minCDE zapC-Slm260

filamentous

Morphology

suppressed by ectopic expression of zapC

Microscopy

Figure 2

edit table

</protect>

Notes

References

See Help:References for how to manage references in omp dev.

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