A physical and functional interaction between escherichia coli FtsK and topoisomerase IV Journal Article
| Authors: | Espeli, O.; Lee, C.; Marians, K. J. |
| Article Title: | A physical and functional interaction between escherichia coli FtsK and topoisomerase IV |
| Abstract: | FtsK and topoisomerase (Topo) IV are both involved in chromosome segregation in Escherichia coli. The former protein resides at the septal ring and is required for resolution of chromosome dimers. The latter protein is the chromosomal decatenase. We have demonstrated recently that Topo IV activity is concentrated at the septal proximal regions of the nucleoids late in the cell cycle. Here we demonstrate that FtsK and Topo IV physically and functionally interact. Topo IV was recovered in immunoprecipitates of FtsK. Two-hybrid analysis and immunoblotting showed that this interaction was mediated by the ParC subunit of Topo IV. In addition, we show that the C-terminal motor domain of FtsK stimulates the decatenation activity of Topo IV but not that of DNA gyrase, the other type II topoisomerase in the cell. Topo IV and FtsK appear to cooperate in the cell as well. Rescue of a pare temperature-sensitive mutation by overproduction of DnaX, which leads to stabilization of the temperature-sensitive Topo IV, required both the C-terminal domain of FtsK and dif, whereas rescue by overproduction of Topo III, which bypasses Topo IV function, did not. The interaction between FtsK and Topo IV may provide a means for concentrating the latter enzyme at the cell center. |
| Keywords: | controlled study; unclassified drug; mutation; nonhuman; protein function; mouse; cell cycle; gene expression; carboxy terminal sequence; protein protein interaction; membrane proteins; enzyme activity; bacteria (microorganisms); bacterial protein; bacterial proteins; dna; recombinant fusion proteins; saccharomyces cerevisiae; escherichia coli; peptide fragments; peptides; immunoprecipitation; immunoblotting; cellular distribution; temperature; dimerization; glucose; protein subunit; dna topoisomerase (atp hydrolysing); enzyme subunit; two hybrid system; temperature sensitivity; drug interactions; enzymes; chromosomes; dna topoisomerase iv; protein parc; chromosome segregation; escherichia coli proteins; dna topoisomerase; two-hybrid system techniques; stimulation; enzyme stability; dimer; protein dif; prokaryota; decatenation; dna topoisomerase iii; protein ftsk; dimers; negibacteria; thermal effects; immunosorbent techniques; precipitation (chemical); priority journal; article; dna gyrase; dnax; arabinose |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 278 |
| Issue: | 45 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2003-11-07 |
| Start Page: | 44639 |
| End Page: | 44644 |
| Language: | English |
| DOI: | 10.1074/jbc.M308926200 |
| PUBMED: | 12939258 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Source: Scopus |
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