A dual role for the FtsK protein in Escherichia coli chromosome segregation.

EMBO Rep

Laboratoire de Microbiologie et de Génétique Moléculaire du CNRS, 118, route de Narbonne, 31062 Toulouse Cedex, France.

Published: June 2002

FtsK is a multifunctional protein that acts in Escherichia coli cell division and chromosome segregation. Its C-terminal domain is required for XerCD-mediated recombination between dif sites that resolve chromosome dimers formed by recombination between sister chromosomes. We report the construction and analysis of a set of strains carrying different Xer recombination sites in place of dif, some of which recombine in an FtsK-independent manner. The results show that FtsK-independent Xer recombination does not support chromosome dimer resolution. Furthermore, resolution of dimers by the Cre/loxP system also requires FtsK. These findings reveal a second role for FtsK during chromosome dimer resolution in addition to XerCD activation. We propose that FtsK acts to position the dif regions, thus allowing a productive synapse between dif sites.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1084150PMC
http://dx.doi.org/10.1093/embo-reports/kvf116DOI Listing

Publication Analysis

Top Keywords

role ftsk
8
escherichia coli
8
chromosome segregation
8
dif sites
8
xer recombination
8
chromosome dimer
8
dimer resolution
8
ftsk
5
chromosome
5
dual role
4

Similar Publications

Structural maintenance of chromosomes (SMC) are ubiquitously distributed proteins involved in chromosome organization. Deletion of causes severe growth phenotypes in many organisms. Surprisingly, can be deleted in , a member of the phylum, without any apparent growth phenotype.

View Article and Find Full Text PDF

Nucleocytoplasmic large DNA viruses (NCLDVs) have massive genome and particle sizes compared to other known viruses. NCLDVs, including poxviruses, encode ATPases of the FtsK/HerA superfamily to facilitate genome encapsidation. However, their biochemical and structural characteristics are yet to be discerned.

View Article and Find Full Text PDF

This study investigates the biodegradation of methyl parathion, an organophosphate pesticide used in paddy fields. Microbial degradation transforms toxic pesticides into less harmful compounds, influenced by the microbial community in the soil. To isolate different microbial colonies, soil samples from an organophosphorus-treated groundnut field were plated on nutrient agar and MSM with 1% glucose and 0.

View Article and Find Full Text PDF
Article Synopsis
  • Serovar L2 (Ct) divides through a unique polarized budding process instead of traditional binary fission, due to its lack of FtsZ, a protein common in other bacteria.
  • The assembly of the divisome, essential for cell division, is initiated by FtsK, which forms specific focal points at the site where new daughter cells will emerge, signifying its role in the division process.
  • Research indicates that FtsK is crucial for recruiting other proteins to the divisome, while MreB, though necessary for forming peptidoglycan rings, does not serve as the primary scaffold for divisome assembly.
View Article and Find Full Text PDF

In almost all bacteria, the tubulin-like GTPase FtsZ polymerizes to form a "Z-ring" that marks the site of division. FtsZ recruits other proteins, collectively known as the divisome, that together remodel and constrict the envelope. Constriction is driven by peptidoglycan (PG) cell wall synthesis by the glycosyltransferase FtsW and the transpeptidase FtsI (FtsWI), but these enzymes require activation to function.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!