| Microtubule-like properties of the bacterial actin homolog ParM-R1. | |
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MedLine Citation:
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PMID: 22908230 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In preparation for mammalian cell division, microtubules repeatedly probe the cytoplasm to capture chromosomes and assemble the mitotic spindle. Critical features of this microtubule system are the formation of radial arrays centered at the centrosomes and dynamic instability, leading to persistent cycles of polymerization and depolymerization. Here, we show that actin homolog, ParM-R1 that drives segregation of the R1 multidrug resistance plasmid from Escherichia coli, can also self-organize in vitro into asters, which resemble astral microtubules. ParM-R1 asters grow from centrosome-like structures consisting of interconnected nodes related by a pseudo 8-fold symmetry. In addition, we show that ParM-R1 is able to perform persistent microtubule-like oscillations of assembly and disassembly. In vitro, a whole population of ParM-R1 filaments is synchronized between phases of growth and shrinkage, leading to prolonged synchronous oscillations even at physiological ParM-R1 concentrations. These results imply that the selection pressure to reliably segregate DNA during cell division has led to common mechanisms within diverse segregation machineries. |
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Authors:
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David Popp; Akihiro Narita; Lin Jie Lee; Mårten Larsson; Robert C Robinson |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-08-20 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 287 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-29 Completed Date: 2013-01-07 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 37078-88 Citation Subset: IM |
Affiliation:
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Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, 138673, Singapore. dpopp@imcb.a-star.edu.sg |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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chemistry*,
genetics,
ultrastructure Adenosine Triphosphate / chemistry Amino Acid Substitution Escherichia coli* Escherichia coli Proteins / chemistry*, genetics, ultrastructure Fourier Analysis Guanosine Triphosphate / chemistry Hydrolysis Light Microtubules / chemistry* Mutagenesis, Site-Directed Protein Multimerization Protein Structure, Quaternary Scattering, Radiation |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Escherichia coli Proteins; 0/ParM protein, E coli; 56-65-5/Adenosine Triphosphate; 86-01-1/Guanosine Triphosphate |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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