Difference between revisions of "PMID:15916962"
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+ | {{RightTOC}} | ||
+ | <!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.829.L4d9c90148d8d0--> | ||
+ | <!-- | ||
+ | ****************************************************************************************** | ||
+ | * | ||
+ | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
+ | * | ||
+ | ****************************************************************************************** --> | ||
+ | {| id="L4d9c90148d8d0" class=" tableEdit PMID_info_table" | ||
+ | |||
+ | |- | ||
+ | !align=left |Citation | ||
+ | || | ||
+ | '''Bernhardt, TG and de Boer, PA''' (2005) SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.''Mol. Cell'' '''18''':555-64 | ||
+ | |- | ||
+ | !align=left |Abstract | ||
+ | || | ||
+ | Cell division in Escherichia coli begins with assembly of the tubulin-like FtsZ protein into a ring structure just underneath the cell membrane. Spatial control over Z ring assembly is achieved by two partially redundant negative regulatory systems, the Min system and nucleoid occlusion (NO), which cooperate to position the division site at midcell. In contrast to the well-studied Min system, almost nothing is known about how Z ring assembly is blocked in the vicinity of nucleoids to effect NO. Reasoning that Min function might become essential in cells impaired for NO, we screened for mutations synthetically lethal with a defective Min system (slm mutants). By using this approach, we identified SlmA (Ttk) as the first NO factor in E. coli. Our combined genetic, cytological, and biochemical results suggest that SlmA is a DNA-associated division inhibitor that is directly involved in preventing Z ring assembly on portions of the membrane surrounding the nucleoid. | ||
+ | |- | ||
+ | !align=left |Links | ||
+ | || | ||
+ | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15916962 PubMed] | ||
+ | Online version:[http://dx.doi.org/10.1016/j.molcel.2005.04.012 10.1016/j.molcel.2005.04.012] | ||
+ | |- | ||
+ | !align=left |Keywords | ||
+ | || | ||
+ | Carrier Proteins; Cell Division; Cell Membrane; Chromosomes, Bacterial; DNA Mutational Analysis; Escherichia coli; Escherichia coli Proteins; Recombinant Fusion Proteins | ||
+ | |||
+ | |- class="tableEdit_footer" | ||
+ | |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.829.L4d9c90148d8d0&page=829&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | ||
+ | |} | ||
+ | <!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.829.L4d9c90148d8d0--> | ||
+ | |||
+ | ==Main Points of the Paper == | ||
+ | *''slmA'' is synthetically lethal with ''minB'' | ||
+ | *Nucleoid cutting results in ''slmA'' mutants, indicating SlmA has a role in septal ring positioning | ||
+ | |||
+ | == Materials and Methods Used == | ||
+ | {{LitMaterials}} | ||
+ | |||
+ | ==Phenotype Annotations== | ||
+ | {{AnnotationTableHelp}} | ||
+ | <protect><!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.829.Y4d9c9014a98f7--> | ||
+ | <!-- | ||
+ | ****************************************************************************************** | ||
+ | * | ||
+ | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
+ | * | ||
+ | ****************************************************************************************** --> | ||
+ | {| id="Y4d9c9014a98f7" class=" tableEdit PMID_Phenotype_table" | ||
+ | |- | ||
+ | !|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes | ||
+ | |- | ||
+ | | | ||
+ | ''Escherichia coli'' | ||
+ | | | ||
+ | |||
+ | | | ||
+ | TB86 | ||
+ | | | ||
+ | slmA minB | ||
+ | | | ||
+ | *filamentation | ||
+ | *absent septation | ||
+ | | | ||
+ | Morphology | ||
+ | | | ||
+ | |||
+ | | | ||
+ | Microscopy | ||
+ | | | ||
+ | Figure 1 and 2 | ||
+ | |- | ||
+ | | | ||
+ | ''Escherichia coli'' | ||
+ | | | ||
+ | |||
+ | | | ||
+ | TB105 | ||
+ | | | ||
+ | ''slmA'' | ||
+ | | | ||
+ | nucleoid cutting/guillotining | ||
+ | |||
+ | | | ||
+ | Morphology | ||
+ | | | ||
+ | septal rings form and constrict over regions of DNA | ||
+ | | | ||
+ | Microscopy | ||
+ | | | ||
+ | Figure 3 | ||
+ | |- | ||
+ | | | ||
+ | ''Escherichia coli'' | ||
+ | | | ||
+ | |||
+ | | | ||
+ | TB86 | ||
+ | | | ||
+ | slmA minB | ||
+ | | | ||
+ | no growth | ||
+ | | | ||
+ | Morphology | ||
+ | | | ||
+ | synthetic lethality | ||
+ | | | ||
+ | Microscopy | ||
+ | | | ||
+ | Figure 1 | ||
+ | |- | ||
+ | | | ||
+ | ''Escherichia coli'' | ||
+ | | | ||
+ | |||
+ | | | ||
+ | TB105 | ||
+ | | | ||
+ | ''slmA'' | ||
+ | | | ||
+ | nucleoid free cells | ||
+ | |||
+ | | | ||
+ | Morphology | ||
+ | | | ||
+ | |||
+ | | | ||
+ | Microscopy | ||
+ | | | ||
+ | Figure 3 | ||
+ | |||
+ | |- class="tableEdit_footer" | ||
+ | |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.829.Y4d9c9014a98f7&page=829&pagename={{FULLPAGENAMEE}}&type=0&template=PMID_Phenotype_table edit table]</span> || || || || || || || || | ||
+ | |} | ||
+ | <!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.829.Y4d9c9014a98f7--></protect> | ||
+ | |||
+ | ==Notes== | ||
+ | |||
+ | ==References== | ||
+ | {{RefHelp}} | ||
+ | <references/> | ||
+ | |||
+ | [[Category:Publication]] | ||
+ | [[Category:To Be Converted]] |
Latest revision as of 12:08, 22 June 2011
Citation |
Bernhardt, TG and de Boer, PA (2005) SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.Mol. Cell 18:555-64 |
---|---|
Abstract |
Cell division in Escherichia coli begins with assembly of the tubulin-like FtsZ protein into a ring structure just underneath the cell membrane. Spatial control over Z ring assembly is achieved by two partially redundant negative regulatory systems, the Min system and nucleoid occlusion (NO), which cooperate to position the division site at midcell. In contrast to the well-studied Min system, almost nothing is known about how Z ring assembly is blocked in the vicinity of nucleoids to effect NO. Reasoning that Min function might become essential in cells impaired for NO, we screened for mutations synthetically lethal with a defective Min system (slm mutants). By using this approach, we identified SlmA (Ttk) as the first NO factor in E. coli. Our combined genetic, cytological, and biochemical results suggest that SlmA is a DNA-associated division inhibitor that is directly involved in preventing Z ring assembly on portions of the membrane surrounding the nucleoid. |
Links |
PubMed Online version:10.1016/j.molcel.2005.04.012 |
Keywords |
Carrier Proteins; Cell Division; Cell Membrane; Chromosomes, Bacterial; DNA Mutational Analysis; Escherichia coli; Escherichia coli Proteins; Recombinant Fusion Proteins |
edit table |
Main Points of the Paper
- slmA is synthetically lethal with minB
- Nucleoid cutting results in slmA mutants, indicating SlmA has a role in septal ring positioning
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 |
TB86 |
slmA minB |
|
Morphology |
Microscopy |
Figure 1 and 2 | ||
Escherichia coli |
TB105 |
slmA |
nucleoid cutting/guillotining |
Morphology |
septal rings form and constrict over regions of DNA |
Microscopy |
Figure 3 | |
Escherichia coli |
TB86 |
slmA minB |
no growth |
Morphology |
synthetic lethality |
Microscopy |
Figure 1 | |
Escherichia coli |
TB105 |
slmA |
nucleoid free cells |
Morphology |
Microscopy |
Figure 3 | ||
edit table |
</protect>
Notes
References
See Help:References for how to manage references in omp dev.