ArticleProceedings of the National Academy of Sciences of the United States of America2016
Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Investigation of artificial cells containing the Par system for bacterial plasmid segregation and inheritance mimicry.Nature communications · 2024Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- The structure of a 15-stranded actin-like filament from Clostridium botulinum.Nature communications · 2019Article
- Nuclear actin: ancient clue to evolution in eukaryotes?Histochemistry and cell biology · 2018Review
- Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Evolution of polymer formation within the actin superfamily.Molecular biology of the cell · 2017Review
- Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution.Protein science : a publication of the Protein Society · 2017Article
- Structural complexity of filaments formed from the actin and tubulin folds.Communicative & integrative biology · 2016Review
- Impact of taxanes on androgen receptor signaling.Asian journal of andrologyReview
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here we report the discovery of a bacterial DNA-segregating actin-like protein (BtParM) from Bacillus thuringiensis, which forms novel antiparallel, two-stranded, supercoiled, nonpolar helical filaments, as determined by electron microscopy. The BtParM filament features of supercoiling and forming antiparallel double-strands are unique within the actin fold superfamily, and entirely different to the straight, double-stranded, polar helical filaments of all other known ParMs and of eukaryotic F-actin. The BtParM polymers show dynamic assembly and subsequent disassembly in the presence of ATP. BtParR, the DNA-BtParM linking protein, stimulated ATP hydrolysis/phosphate release by BtParM and paired two supercoiled BtParM filaments to form a cylinder, comprised of four strands with inner and outer diameters of 57 Å and 145 Å, respectively. Thus, in this prokaryote, the actin fold has evolved to produce a filament system with comparable features to the eukaryotic chromosome-segregating microtubule.
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