Document Detail

Microtubule-like properties of the bacterial actin homolog ParM-R1.
MedLine Citation:
PMID:  22908230     Owner:  NLM     Status:  MEDLINE    
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.
David Popp; Akihiro Narita; Lin Jie Lee; Mårten Larsson; Robert C Robinson
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-08-20
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  287     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-29     Completed Date:  2013-01-07     Revised Date:  2013-11-05    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  37078-88     Citation Subset:  IM    
Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, 138673, Singapore.
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MeSH Terms
Actins / chemistry*,  genetics,  ultrastructure
Adenosine Triphosphate / chemistry
Amino Acid Substitution
Escherichia coli*
Escherichia coli Proteins / chemistry*,  genetics,  ultrastructure
Fourier Analysis
Guanosine Triphosphate / chemistry
Microtubules / chemistry*
Mutagenesis, Site-Directed
Protein Multimerization
Protein Structure, Quaternary
Scattering, Radiation
Reg. No./Substance:
0/Actins; 0/Escherichia coli Proteins; 0/ParM protein, E coli; 56-65-5/Adenosine Triphosphate; 86-01-1/Guanosine Triphosphate

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