A5000138070- Bacterial Genetics and Biotechnology
- Antibiotic Resistance in Bacteria
- RNA and protein synthesis mechanisms
- Escherichia coli research studies
- Legume Nitrogen Fixing Symbiosis
- DNA Repair Mechanisms
Philipps University of Marburg
2021-2024
Max Planck Institute for Terrestrial Microbiology
2023
ParB-like CTPases mediate the segregation of bacterial chromosomes and low-copy number plasmids. They act as DNA-sliding clamps that are loaded at parS motifs in centromere target DNA molecules spread laterally to form large nucleoprotein complexes serving docking points for machinery. Here, we solve crystal structures ParB pre- post-hydrolysis state illuminate catalytic mechanism nucleotide hydrolysis. Moreover, identify conformational changes underlie CTP- parS-dependent closure clamps....
Abstract The transcriptional antisilencer VirB acts as a master regulator of virulence gene expression in the human pathogen Shigella flexneri . It binds DNA sequences ( virS ) upstream VirB-dependent promoters and counteracts their silencing by nucleoid-organizing protein H-NS. However, its precise mode action remains unclear. Notably, is not classical transcription factor but related to ParB-type DNA-partitioning proteins, which have recently been recognized DNA-sliding clamps using CTP...
DNA segregation by bacterial ParABS systems is mediated transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes clamp-forming CTPase ParB. The lifetime these limited ParB-dependent activation activity. Here, we elucidate functional interplay ParB in model bacterium Myxococcus xanthus. We demonstrate that N-terminal ParA-binding motif associates with a conserved bipartite binding pocket at dimer interface, manner dependent...
Abstract The transcriptional antisilencer VirB acts as a master regulator of virulence gene expression in the human pathogen Shigella flexneri . It binds defined sequences ( virS ) upstream VirB-dependent promoters and counteracts their silencing by nucleoid-organizing protein H-NS. However, its precise mode action remains unclear. Notably, is not classical transcription factor but related to DNA partitioning proteins ParB family, which have recently been recognized DNA-sliding clamps using...
SUMMARY DNA partitioning CTPases of the ParB family mediate segregation bacterial chromosomes and low-copy number plasmids. They act as DNA-sliding clamps that are loaded at parS motifs in centromeric region target molecules then spread laterally to form large nucleoprotein complexes serve docking points for machinery. Here, we identify conformational changes underlie CTP- -dependent closure clamps. Moreover, solve crystal structures pre- post-hydrolysis state provide insights into catalytic...