The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
| Autor: | Alexandra V. Parker, Svetomir B. Tzokov, Julien R. C. Bergeron, Daniel Mann, Ling Chin Hwang |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
DNA
Bacterial Cell division Protein Conformation Science General Physics and Astronomy Vibrio cholerae/chemistry macromolecular substances Crystallography X-Ray Genome General Biochemistry Genetics and Molecular Biology DNA sequencing Article Protein filament Quantitative Biology::Subcellular Processes chemistry.chemical_compound Bacterial Proteins Bacterial Proteins/chemistry Chromosome Segregation DNA Bacterial/chemistry Physics::Atomic and Molecular Clusters Nucleoid Nucleotide Physics::Chemical Physics Cellular microbiology Vibrio cholerae chemistry.chemical_classification Adenosine Triphosphatases Bacterial structural biology Quantitative Biology::Biomolecules Multidisciplinary Chemistry Cryoelectron Microscopy Cooperative binding General Chemistry Quantitative Biology::Genomics Chromosome segregation Adenosine Triphosphatases/chemistry Biophysics Nucleic Acid Conformation ddc:500 DNA |
| Zdroj: | Parker, A V, Mann, D, Tzokov, S B, Hwang, L C & Bergeron, J R C 2021, ' The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding ', Nature Communications, vol. 12, no. 1, 5166 . https://doi.org/10.1038/s41467-021-25429-2 Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021) Nature Communications Nature Communications 12, 5166 (2021). doi:10.1038/s41467-021-25429-2 |
| ISSN: | 2041-1723 |
| Popis: | The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA’s cooperative binding to DNA and the formation of high ParA density regions on the nucleoid. ParA is an ATPase involved in the segregation of newly replicated DNA in bacteria. Here, structures of a ParA filament bound to DNA and of ParA in various nucleotide states offer insight into its conformational changes upon DNA binding and filament assembly, including the basis for ParA’s cooperative binding to DNA. |
| Databáze: | OpenAIRE |
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