ArticleThe Journal of biological chemistry2012
Novel actin-like filament structure from Clostridium tetani.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Polymer dynamics of Alp7A reveals how two critical concentrations govern assembly of dynamically unstable actin-like proteins.Molecular biology of the cell · 2024Article
- Archaeal actins and the origin of a multi-functional cytoskeleton.Journal of bacteriology · 2024Review
- 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
- Virulence Plasmids of the Pathogenic Clostridia.Microbiology spectrum · 2019Article
- A protein self-assembly model guided by electrostatic and hydrophobic dipole moments.PloS one · 2019Article
- Prokaryotic cytoskeletons: protein filaments organizing small cells.Nature reviews. Microbiology · 2018Review
- Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution.Protein science : a publication of the Protein Society · 2017Article
- 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 · 2016Article
- Structural complexity of filaments formed from the actin and tubulin folds.Communicative & integrative biology · 2016Review
- Article
- In search of the primordial actin filament.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Virulence Plasmids of Spore-Forming Bacteria.Microbiology spectrum · 2014Review
- Article
- Bacterial actins and their diversity.Biochemistry · 2013Review
- Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013Article
- The bacterial actin MamK: in vitro assembly behavior and filament architecture.The Journal of biological chemistry · 2013Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic F-actin is constructed from two protofilaments that gently wind around each other to form a helical polymer. Several bacterial actin-like proteins (Alps) are also known to form F-actin-like helical arrangements from two protofilaments, yet with varied helical geometries. Here, we report a unique filament architecture of Alp12 from Clostridium tetani that is constructed from four protofilaments. Through fitting of an Alp12 monomer homology model into the electron microscopy data, the filament was determined to be constructed from two antiparallel strands, each composed of two parallel protofilaments. These four protofilaments form an open helical cylinder separated by a wide cleft. The molecular interactions within single protofilaments are similar to F-actin, yet interactions between protofilaments differ from those in F-actin. The filament structure and assembly and disassembly kinetics suggest Alp12 to be a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin, and thus a potential target for drug design. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.
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