Evidence map›Paper›PMID 20106979›Full record

ArticleThe Journal of biological chemistry2010

Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation.

David Popp, Weijun Xu, Akihiro Narita, Anthony J Brzoska, Ronald A Skurray, Neville Firth, Umesh Goshdastider, Yuichiro Maéda, Robert C Robinson, Maria A Schumacher

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. Transposition of TnAntimicrobial agents and chemotherapy · 2025
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  9. Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Review
  11. Article
  12. Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Goshdastider, Umesh [corrected to Ghoshdastider, Umesh]
5 · Who and what money

Authors and funding

10 authors at 4 institutions in 4 countries.

David PoppERATO "Actin Filament Dynamics" Project, Japan Science and Technology Corporation, c/o RIKEN, Harima Institute at Spring 8, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan; Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos 138673, Singapore. Electronic address: dpopp@imcb.A-star.edu.sg.
Weijun XuDepartment of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030.
Akihiro NaritaERATO "Actin Filament Dynamics" Project, Japan Science and Technology Corporation, c/o RIKEN, Harima Institute at Spring 8, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan; Nagoya University Graduate School of Science, Structural Biology Research Center and Division of Biological Sciences, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Anthony J BrzoskaSchool of Biological Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Ronald A SkurraySchool of Biological Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Neville FirthSchool of Biological Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Umesh GoshdastiderNagoya University Graduate School of Science, Structural Biology Research Center and Division of Biological Sciences, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Yuichiro MaédaERATO "Actin Filament Dynamics" Project, Japan Science and Technology Corporation, c/o RIKEN, Harima Institute at Spring 8, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan; Nagoya University Graduate School of Science, Structural Biology Research Center and Division of Biological Sciences, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Robert C RobinsonInstitute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos 138673, Singapore.
Maria A SchumacherDepartment of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030. Electronic address: maschuma@mdanderson.org.
Nagoya University · JPUniversity of Sydney · AUInstitute of Molecular and Cell Biology · SGThe University of Texas MD Anderson Cancer Center · US

Funding

Structural mechanism of DNA segregation by the pSK41 par systemR01AI080687 · NIAID · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SCHUMACHER, MARIA · 2009 to 2010
$693k
NIAID NIH HHS R01 AI080687
6 · The paper itself

Abstract

Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The Staphylococcus aureus pSK41 plasmid is a medically important plasmid that confers resistance to multiple antibiotics, disinfectants, and antiseptics. In the first step of partition, the pSK41 ParR binds its DNA centromere to form a superhelical partition complex that recruits ParM, which then mediates plasmid separation. pSK41 ParM is homologous to R1 ParM, a known actin homologue, suggesting that it may also form filaments to drive partition. To gain insight into the partition function of ParM, we examined its ability to form filaments and determined the crystal structure of apoParM to 1.95 A. The structure shows that pSK41 ParM belongs to the actin/Hsp70 superfamily. Unexpectedly, however, pSK41 ParM shows the strongest structural homology to the archaeal actin-like protein Thermoplasma acidophilum Ta0583, rather than its functional homologue, R1 ParM. Consistent with this divergence, we find that regions shown to be involved in R1 ParM filament formation are not important in formation of pSK41 ParM polymers. These data are also consonant with our finding that pSK41 ParM forms 1-start 10/4 helices very different from the 37/17 symmetry of R1 ParM. The polymerization kinetics of pSK41 ParM also differed from that of R1 ParM. These results indicate that type II NTPases utilize different polymeric structures to drive plasmid segregation.

Indexed as

ActinsBacterial ProteinsCentromereCrystallography, X-RayDNAFourier AnalysisHistonesKineticsMicroscopy, FluorescencePlasmidsProtein ConformationProtein Interaction MappingStaphylococcus aureusStatic ElectricityThermoplasmaActinsBacterial ProteinsDNAHistones

Identifiers

PMID20106979
PMCPMC2843175
OpenAlexW2007254915

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.