Evidence map›Paper›PMID 23204522›Full record

ArticleThe Journal of biological chemistry2013

The bacterial actin MamK: in vitro assembly behavior and filament architecture.

Ertan Ozyamak, Justin Kollman, David A Agard, Arash Komeili

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

44 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  6. A family of bacterial actin homologs forms a three-stranded tubular structure.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
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  10. bioRxiv : the preprint server for biology · 2023
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  15. Metabolic characterisation ofRSC advances · 2020
    Article
  16. Review
  17. Cryo-EM reconstruction of AlfA fromProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
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  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Ertan OzyamakDepartment of Plant and Microbial Biology, University of California, Berkeley, California 94720, USA.
Justin Kollman
David A Agard
Arash Komeili
University of California, Berkeley · USMcGill University · CAUniversity of California, San Francisco · US

Funding

Microtubule Nucleation: Structure & MechanismR01GM031627 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 1985 to 2016
$6.1M
Molecular Mechanisms of Organelle Assembly by the Prokaryotic Actin Homolog MamKR01GM084122 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOMEILI, ARASH · 2009 to 2017
$2.8M
Howard Hughes Medical InstituteNIGMS NIH HHS GM031627NIGMS NIH HHS R01 GM031627NIGMS NIH HHS R01 GM084122NIGMS NIH HHS R01GM084122
6 · The paper itself

Abstract

It is now recognized that actin-like proteins are widespread in bacteria and, in contrast to eukaryotic actins, are highly diverse in sequence and function. The bacterial actin, MamK, represents a clade, primarily found in magnetotactic bacteria, that is involved in the proper organization of subcellular organelles, termed magnetosomes. We have previously shown that MamK from Magnetospirillum magneticum AMB-1 (AMB-1) forms dynamic filaments in vivo. To gain further insights into the molecular mechanisms that underlie MamK dynamics and function, we have now studied the in vitro properties of MamK. We demonstrate that MamK is an ATPase that, in the presence of ATP, assembles rapidly into filaments that disassemble once ATP is depleted. The mutation of a conserved active site residue (E143A) abolishes ATPase activity of MamK but not its ability to form filaments. Filament disassembly depends on both ATPase activity and potassium levels, the latter of which results in the organization of MamK filaments into bundles. These data are consistent with observations indicating that accessory factors are required to promote filament disassembly and for spatial organization of filaments in vivo. We also used cryo-electron microscopy to obtain a high resolution structure of MamK filaments. MamK adopts a two-stranded helical filament architecture, but unlike eukaryotic actin and other actin-like filaments, subunits in MamK strands are unstaggered giving rise to a unique filament architecture. Beyond extending our knowledge of the properties and function of MamK in magnetotactic bacteria, this study emphasizes the functional and structural diversity of bacterial actins in general.

Indexed as

Actin CytoskeletonActinsAdenosine TriphosphatasesAmino Acid SubstitutionBacterial ProteinsMagnetospirillumMutation, MissenseActinsAdenosine TriphosphatasesBacterial Proteins

Identifiers

PMID23204522
PMCPMC3567678
OpenAlexW1966350338

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.