A CTP-dependent gating mechanism enables ParB spreading on DNA
Autor: | Anjana Badrinarayanan, Ngat T. Tran, Afroze Chimthanawala, Clare E. M. Stevenson, Adam S. B. Jalal, David M. Lawson, Tung B. K. Le |
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Rok vydání: | 2021 |
Předmět: |
DNA
Bacterial Cytidine triphosphate QH301-705.5 Science Cytidine Triphosphate chromosome segregation Nucleation ParA ParB parS Gating General Biochemistry Genetics and Molecular Biology Chromosome segregation 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Bacterial Proteins Protein Domains Caulobacter crescentus Compartment (development) Biology (General) 030304 developmental biology 0303 health sciences General Immunology and Microbiology biology Chemistry Hydrolysis General Neuroscience 030302 biochemistry & molecular biology General Medicine Chromosomes and Gene Expression biology.organism_classification CTP Biophysics Medicine Research Advance spreading Crystallization molecular gates 030217 neurology & neurosurgery DNA Protein Binding |
Zdroj: | eLife eLife, Vol 10 (2021) |
ISSN: | 2050-084X |
DOI: | 10.7554/elife.69676 |
Popis: | Proper chromosome segregation is essential in all living organisms. The ParA-ParB-parS system is widely employed for chromosome segregation in bacteria. Previously, we showed that Caulobacter crescentus ParB requires cytidine triphosphate to escape the nucleation site parS and spread by sliding to the neighboring DNA 1. Here, we provide the structural basis for this transition from nucleation to spreading by solving co-crystal structures of a C-terminal domain truncated C. crescentus ParB with parS and with a CTP analog. Nucleating ParB is an open clamp, in which parS is captured at the DNA-binding domain (the DNA-gate). Upon binding CTP, the N-terminal domain (NTD) self-dimerizes to close the NTD-gate of the clamp. The DNA-gate also closes, thus driving parS into a compartment between the DNA-gate and the C-terminal domain. CTP hydrolysis and/or the release of hydrolytic products are likely associated with re-opening of the gates to release DNA and to recycle ParB. Overall, we suggest a CTP-operated gating mechanism that regulates ParB nucleation, spreading, and recycling. |
Databáze: | OpenAIRE |
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