Article abstract
Nature Structural & Molecular Biology 14, 921 - 926 (2007)
Published online: 16 September 2007 | doi:10.1038/nsmb1300
The structure of bacterial ParM filaments
Albina Orlova1, Ethan C Garner2, Vitold E Galkin1, John Heuser3, R Dyche Mullins2 & Edward H Egelman1
Abstract
Bacterial ParM is a homolog of eukaryotic actin and is involved in moving plasmids so that they segregate properly during cell division. Using cryo-EM and three-dimensional reconstruction, we show that ParM filaments have a different structure from F-actin, with very different subunit-subunit interfaces. These interfaces result in the helical handedness of the ParM filament being opposite to that of F-actin. Like F-actin, ParM filaments have a variable twist, and we show that this involves domain-domain rotations within the ParM subunit. The present results yield new insights into polymorphisms within F-actin, as well as the evolution of polymer families.
- Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-0733, USA.
- Department of Cellular and Molecular Pharmacology, University of California San Francisco Medical School, San Francisco, California 94107, USA.
- Department of Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Correspondence to: Edward H Egelman1 e-mail: egelman@virginia.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Actin allostery again?Nature Structural Biology News and Views (01 Sep 2001)
Cell biology: Muscle au naturelNature News and Views (10 Nov 1983)
RESEARCH
Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instabilityThe EMBO Journal Article
Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instabilityThe EMBO Journal Article (06 Feb 2008)
See all 52 matches for Research
