ArticleThe EMBO journal2010
Fully efficient chromosome dimer resolution in Escherichia coli cells lacking the integral membrane domain of FtsK.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Interplay between the Xer recombination system and the dissemination of antibioresistance in Acinetobacter baumannii.Nucleic acids research · 2025Article
- Article
- Transient enhanced cell division by blocking DNA synthesis inMicrobiology (Reading, England) · 2020Article
- Characterization of the Chromosome Dimer Resolution Site in Caulobacter crescentus.Journal of bacteriology · 2019Article
- The TLCΦ satellite phage harbors a Xer recombination activation factor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Outer membrane lipoprotein RlpA is a novel periplasmic interaction partner of the cell division protein FtsK in Escherichia coli.Scientific reports · 2018Article
- Sequence-dependent catalytic regulation of the SpoIIIE motor activity ensures directionality of DNA translocation.Scientific reports · 2018Article
- Late assembly of the Vibrio cholerae cell division machinery postpones septation to the last 10% of the cell cycle.Scientific reports · 2017Article
- Fast growth conditions uncouple the final stages of chromosome segregation and cell division in Escherichia coli.PLoS genetics · 2017Article
- Differential management of the replication terminus regions of the two Vibrio cholerae chromosomes during cell division.PLoS genetics · 2014Article
- Site-directed fluorescence labeling reveals a revised N-terminal membrane topology and functional periplasmic residues in the Escherichia coli cell division protein FtsK.The Journal of biological chemistry · 2014Article
- Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA.Molecular cell · 2014Article
- TPM analyses reveal that FtsK contributes both to the assembly and the activation of the XerCD-dif recombination synapse.Nucleic acids research · 2014Article
- Structural studies of planctomycete Gemmata obscuriglobus support cell compartmentalisation in a bacterium.PloS one · 2014Article
- In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division.The Journal of biological chemistry · 2013Review
- Recruitment, assembly, and molecular architecture of the SpoIIIE DNA pump revealed by superresolution microscopy.PLoS biology · 2013Article
- Molecular motors for DNA translocation in prokaryotes.Current opinion in biotechnology · 2012Review
- A septal chromosome segregator protein evolved into a conjugative DNA-translocator protein.Mobile genetic elements · 2011Article
- Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE.The EMBO journal · 2011Article
- Comprehensive prediction of chromosome dimer resolution sites in bacterial genomes.BMC genomics · 2011Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, septum formation frequently initiates before the last steps of chromosome segregation. This is notably the case when chromosome dimers are formed by homologous recombination. Chromosome segregation then requires the activity of a double-stranded DNA transporter anchored at the septum by an integral membrane domain, FtsK. It was proposed that the transmembrane segments of proteins of the FtsK family form pores across lipid bilayers for the transport of DNA. Here, we show that truncated Escherichia coli FtsK proteins lacking all of the FtsK transmembrane segments allow for the efficient resolution of chromosome dimers if they are connected to a septal targeting peptide through a sufficiently long linker. These results indicate that FtsK does not need to transport DNA through a pore formed by its integral membrane domain. We propose therefore that FtsK transports DNA before membrane fusion, at a time when there is still an opening in the constricted septum.
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