PMID:21113127: Difference between revisions
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!align=left |Citation | |||
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'''Tonthat, NK, Arold, ST, Pickering, BF, Van Dyke, MW, Liang, S, Lu, Y, Beuria, TK, Margolin, W and Schumacher, MA''' (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.''EMBO J.'' '''30''':154-64 | |||
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!align=left |Abstract | |||
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In Escherichia coli, cytokinesis is orchestrated by FtsZ, which forms a Z-ring to drive septation. Spatial and temporal control of Z-ring formation is achieved by the Min and nucleoid occlusion (NO) systems. Unlike the well-studied Min system, less is known about the anti-DNA guillotining NO process. Here, we describe studies addressing the molecular mechanism of SlmA (synthetic lethal with a defective Min system)-mediated NO. SlmA contains a TetR-like DNA-binding fold, and chromatin immunoprecipitation analyses show that SlmA-binding sites are dispersed on the chromosome except the Ter region, which segregates immediately before septation. SlmA binds DNA and FtsZ simultaneously, and the SlmA-FtsZ structure reveals that two FtsZ molecules sandwich a SlmA dimer. In this complex, FtsZ can still bind GTP and form protofilaments, but the separated protofilaments are forced into an anti-parallel arrangement. This suggests that SlmA may alter FtsZ polymer assembly. Indeed, electron microscopy data, showing that SlmA-DNA disrupts the formation of normal FtsZ polymers and induces distinct spiral structures, supports this. Thus, the combined data reveal how SlmA derails Z-ring formation at the correct place and time to effect NO. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21113127 PubMed] | |||
Online version:[http://dx.doi.org/10.1038/emboj.2010.288 10.1038/emboj.2010.288] | |||
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!align=left |Keywords | |||
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Bacterial Proteins; Base Sequence; Binding Sites; Carrier Proteins; Chromosomes, Bacterial; Crystallography, X-Ray; Cytokinesis; Cytoskeletal Proteins; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Protein Binding; Protein Conformation; Protein Multimerization; Scattering, Small Angle; X-Ray Diffraction | |||
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==Main Points of the Paper == | |||
*Crystal structure of ''E.coli'' SlmA protein | |||
*SlmA binding sequences (SBS) are identified and their chromosomal distribution is investigated | |||
*Model for SlmA-mediated nucleoid occlusion (NO) is presented | |||
*PDB Accession number- 3NXC | |||
== Materials and Methods Used == | |||
{{LitMaterials}} | |||
==Phenotype Annotations== | |||
{{AnnotationTableHelp}} | |||
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!|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes | |||
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==Notes== | |||
==References== | |||
{{RefHelp}} | |||
<references/> | |||
[[Category:FP Assay]][[Category:FtsZ Protein Purification]][[Category:X-ray Crystallography]][[Category:Microscopy, Electron]][[Category:Chromatin Immunoprecipitation (ChIP)]][[Category:FtsZ Polymerization Assay]][[Category:SAXS]] | |||
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Latest revision as of 17:09, 22 June 2011
| Citation |
Tonthat, NK, Arold, ST, Pickering, BF, Van Dyke, MW, Liang, S, Lu, Y, Beuria, TK, Margolin, W and Schumacher, MA (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.EMBO J. 30:154-64 |
|---|---|
| Abstract |
In Escherichia coli, cytokinesis is orchestrated by FtsZ, which forms a Z-ring to drive septation. Spatial and temporal control of Z-ring formation is achieved by the Min and nucleoid occlusion (NO) systems. Unlike the well-studied Min system, less is known about the anti-DNA guillotining NO process. Here, we describe studies addressing the molecular mechanism of SlmA (synthetic lethal with a defective Min system)-mediated NO. SlmA contains a TetR-like DNA-binding fold, and chromatin immunoprecipitation analyses show that SlmA-binding sites are dispersed on the chromosome except the Ter region, which segregates immediately before septation. SlmA binds DNA and FtsZ simultaneously, and the SlmA-FtsZ structure reveals that two FtsZ molecules sandwich a SlmA dimer. In this complex, FtsZ can still bind GTP and form protofilaments, but the separated protofilaments are forced into an anti-parallel arrangement. This suggests that SlmA may alter FtsZ polymer assembly. Indeed, electron microscopy data, showing that SlmA-DNA disrupts the formation of normal FtsZ polymers and induces distinct spiral structures, supports this. Thus, the combined data reveal how SlmA derails Z-ring formation at the correct place and time to effect NO. |
| Links |
PubMed Online version:10.1038/emboj.2010.288 |
| Keywords |
Bacterial Proteins; Base Sequence; Binding Sites; Carrier Proteins; Chromosomes, Bacterial; Crystallography, X-Ray; Cytokinesis; Cytoskeletal Proteins; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Protein Binding; Protein Conformation; Protein Multimerization; Scattering, Small Angle; X-Ray Diffraction |
| edit table |
Main Points of the Paper
- Crystal structure of E.coli SlmA protein
- SlmA binding sequences (SBS) are identified and their chromosomal distribution is investigated
- Model for SlmA-mediated nucleoid occlusion (NO) is presented
- PDB Accession number- 3NXC
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.
| Species | Taxon ID | Strain | Gene (if known) | OMP | Phenotype | Details | Evidence | Notes |
|---|---|---|---|---|---|---|---|---|
| edit table |
Notes
References
See Help:References for how to manage references in OMPwiki.
