Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus
| Autor: | Binbin He, Gert Bange, Martin Thanbichler, Yacine Refes, Gaël Panis, Laura Corrales-Guerrero, Patrick H. Viollier, Wieland Steinchen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Cell division
AcademicSubjects/SCI00010 ATPase Dimer Hydrogen Deuterium Exchange-Mass Spectrometry Diffusion Chromosome segregation 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Bacterial Proteins Caulobacter crescentus Genetics Nucleoid 030304 developmental biology Adenosine Triphosphatases ddc:616 0303 health sciences Binding Sites biology Gene regulation Chromatin and Epigenetics DNA biology.organism_classification DNA-Binding Proteins DNA binding site chemistry Mutation Biophysics biology.protein 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Nucleic Acids Research (2020) Nucleic Acids Research NUCLEIC ACIDS RESEARCH |
| ISSN: | 0305-1048 |
| Popis: | The spatiotemporal regulation of chromosome segregation and cell division in Caulobacter crescentus is mediated by two different P-loop ATPases, ParA and MipZ. Both of these proteins form dynamic concentration gradients that control the positioning of regulatory targets within the cell. Their proper localization depends on their nucleotide-dependent cycling between a monomeric and a dimeric state and on the ability of the dimeric species to associate with the nucleoid. In this study, we use a combination of genetic screening, biochemical analysis and hydrogen/deuterium exchange mass spectrometry to comprehensively map the residues mediating the interactions of MipZ and ParA with DNA. We show that MipZ has non-specific DNA-binding activity that relies on an array of positively charged and hydrophobic residues lining both sides of the dimer interface. Extending our analysis to ParA, we find that the MipZ and ParA DNA-binding sites differ markedly in composition, although their relative positions on the dimer surface and their mode of DNA binding are conserved. In line with previous experimental work, bioinformatic analysis suggests that the same principles may apply to other members of the P-loop ATPase family. P-loop ATPases thus share common mechanistic features, although their functions have diverged considerably during the course of evolution. |
| Databáze: | OpenAIRE |
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