Global DNA Compaction in Stationary-Phase Bacteria Does Not Affect Transcription
| Autor: | Anne S. Meyer, Natalia N. Vtyurina, Richard Janissen, Nynke H. Dekker, Dick de Ridder, Zaïda Rivai, Mathia M.A. Arens, Behrouz Eslami-Mossallam, Alexey A. Gritsenko, Liedewij Laan, Irina Artsimovitch, Nicholas D. Sunday, Elio A. Abbondanzieri |
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| Rok vydání: | 2018 |
| Předmět: |
DNA
Bacterial 0301 basic medicine nucleoid Proteome Transcription Genetic Bioinformatics single-molecule biophysics 030106 microbiology Biology DNA condensation medicine.disease_cause Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chemistry.chemical_compound Transcription (biology) RNA polymerase Bioinformatica Escherichia coli medicine Nucleoid stationary phase Gene Sequence Analysis RNA Escherichia coli Proteins DNA Restriction Enzymes DNA-Directed RNA Polymerases Gene Expression Regulation Bacterial stress response Cell biology DNA-Binding Proteins Restriction enzyme 030104 developmental biology Microscopy Fluorescence chemistry Polystyrenes bacteria Stress Mechanical Dps EPS Holoenzymes Transcriptome magnetic tweezers transcription DNA Bacterial Outer Membrane Proteins |
| Zdroj: | Cell, 174(5), 1188-1199.e14 Cell 174 (2018) 5 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2018.06.049 |
| Popis: | In stationary-phase Escherichia coli, Dps (DNA-binding protein from starved cells) is the most abundant protein component of the nucleoid. Dps compacts DNA into a dense complex and protects it from damage. Dps has also been proposed to act as a global regulator of transcription. Here, we directly examine the impact of Dps-induced compaction of DNA on the activity of RNA polymerase (RNAP). Strikingly, deleting the dps gene decompacted the nucleoid but did not significantly alter the transcriptome and only mildly altered the proteome during stationary phase. Complementary in vitro assays demonstrated that Dps blocks restriction endonucleases but not RNAP from binding DNA. Single-molecule assays demonstrated that Dps dynamically condenses DNA around elongating RNAP without impeding its progress. We conclude that Dps forms a dynamic structure that excludes some DNA-binding proteins yet allows RNAP free access to the buried genes, a behavior characteristic of phase-separated organelles. Despite markedly condensing the bacterial chromosome, the nucleoid-structuring protein Dps selectively allows access by RNA polymerase and transcription factors at normal rates while excluding other factors such as restriction endonucleases. |
| Databáze: | OpenAIRE |
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