ArticlePloS one2014
Dr-FtsA, an actin homologue in Deinococcus radiodurans differentially affects Dr-FtsZ and Ec-FtsZ functions in vitro.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Phytonutrients as a Defensive Barrier Against G Ectodomain Fusion in Chandipura Virus Infection.Molecular biotechnology · 2026Article
- Comparative genomics ofFrontiers in microbiology · 2024Article
- Article
- FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus.Journal of bacteriology · 2020Article
- Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions inmSphere · 2018Article
- The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-bound FtsZ2.The Journal of biological chemistry · 2018Article
- FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.Molecular microbiology · 2018Article
- Splitsville: structural and functional insights into the dynamic bacterial Z ring.Nature reviews. Microbiology · 2016Review
- DNA Gyrase of Deinococcus radiodurans is characterized as Type II bacterial topoisomerase and its activity is differentially regulated by PprA in vitro.Extremophiles : life under extreme conditions · 2016Article
- Molecular insights into replication initiation in a multipartite genome harboring bacterium Deinococcus radiodurans.The Journal of biological chemistryArticle
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Deinococcus radiodurans genome encodes homologues of divisome proteins including FtsZ and FtsA. FtsZ of this bacterium (Dr-FtsZ) has been recently characterized. In this paper, we study FtsA of D. radiodurans (Dr-FtsA) and its involvement in regulation of FtsZ function. Recombinant Dr-FtsA showed neither ATPase nor GTPase activity and its polymerization was ATP dependent. Interestingly, we observed that Dr-FtsA, when compared with E. coli FtsA (Ec-FtsA), has lower affinity for both Dr-FtsZ and Ec-FtsZ. Also, Dr-FtsA showed differential effects on GTPase activity and sedimentation characteristics of Dr-FtsZ and Ec-FtsZ. For instance, Dr-FtsA stimulated GTPase activity of Dr-FtsZ while GTPase activity of Ec-FtsZ was reduced in the presence of Dr-FtsA. Stimulation of GTPase activity of Dr-FtsZ by Dr-FtsA resulted in depolymerization of Dr-FtsZ. Dr-FtsA effects on GTPase activity and polymerization/depolymerisation characteristics of Dr-FtsZ did not change significantly in the presence of ATP. Recombinant E. coli expressing Dr-FtsA showed cell division inhibition in spite of in trans expression of Dr-FtsZ in these cells. These results suggested that Dr-FtsA, although it lacks ATPase activity, is still functional and differentially affects Dr-FtsZ and Ec-FtsZ function in vitro.
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