FtsZ ring: the eubacterial division apparatus conserved in archaebacteria - PubMed (original) (raw)
FtsZ ring: the eubacterial division apparatus conserved in archaebacteria
X Wang et al. Mol Microbiol. 1996 Jul.
Abstract
FtsZ is a tubulin-like protein that is essential for cell division in eubacteria. It functions by forming a ring at the division site that directs septation. The archaebacteria constitute a kingdom of life separate from eubacteria and eukaryotes. Like eubacteria, archaebacteria are prokaryotes, although they are phylogenetically closer to eukaryotes. Here it is shown that archaebacteria also possess FtsZ and that it is biochemically similar to eubacterial FtsZs. Significantly, FtsZ from the archaebacterium Haloferax volcanii is a GTPase that is localized to a ring that coincides with the division constriction. These results indicate that the FtsZ ring was part of the division apparatus of a common prokaryotic ancestor that was retained by both eubacteria and archaebacteria.
Similar articles
- An archaebacterial homologue of the essential eubacterial cell division protein FtsZ.
Baumann P, Jackson SP. Baumann P, et al. Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6726-30. doi: 10.1073/pnas.93.13.6726. Proc Natl Acad Sci U S A. 1996. PMID: 8692886 Free PMC article. - Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin.
Margolin W, Wang R, Kumar M. Margolin W, et al. J Bacteriol. 1996 Mar;178(5):1320-7. doi: 10.1128/jb.178.5.1320-1327.1996. J Bacteriol. 1996. PMID: 8631708 Free PMC article. - The ftsZ gene of Haloferax mediterranei: sequence, conserved gene order, and visualization of the FtsZ ring.
Poplawski A, Gullbrand B, Bernander R. Poplawski A, et al. Gene. 2000 Jan 25;242(1-2):357-67. doi: 10.1016/s0378-1119(99)00517-x. Gene. 2000. PMID: 10721730 - Bacterial cell division and the Z ring.
Lutkenhaus J, Addinall SG. Lutkenhaus J, et al. Annu Rev Biochem. 1997;66:93-116. doi: 10.1146/annurev.biochem.66.1.93. Annu Rev Biochem. 1997. PMID: 9242903 Review. - Strong FtsZ is with the force: mechanisms to constrict bacteria.
Mingorance J, Rivas G, Vélez M, Gómez-Puertas P, Vicente M. Mingorance J, et al. Trends Microbiol. 2010 Aug;18(8):348-56. doi: 10.1016/j.tim.2010.06.001. Epub 2010 Jul 1. Trends Microbiol. 2010. PMID: 20598544 Review.
Cited by
- Widespread photosynthesis reaction centre barrel proteins are necessary for haloarchaeal cell division.
Zhao S, Makarova KS, Zheng W, Zhan L, Wan Q, Liu Y, Gong H, Krupovic M, Lutkenhaus J, Chen X, Koonin EV, Du S. Zhao S, et al. Nat Microbiol. 2024 Mar;9(3):712-726. doi: 10.1038/s41564-024-01615-y. Epub 2024 Mar 4. Nat Microbiol. 2024. PMID: 38443574 - Archaeal Tubulin-like Proteins Modify Cell Shape in Haloferax volcanii during Early Biofilm Development.
Cooper A, Makkay AM, Papke RT. Cooper A, et al. Genes (Basel). 2023 Sep 25;14(10):1861. doi: 10.3390/genes14101861. Genes (Basel). 2023. PMID: 37895209 Free PMC article. - An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.
Viola MG, Perdikari TM, Trebino CE, Rahmani N, Mathews KL, Pena CM, Chua XY, Xuan B, LaBreck CJ, Fawzi NL, Camberg JL. Viola MG, et al. Protein Sci. 2022 May;31(5):e4306. doi: 10.1002/pro.4306. Protein Sci. 2022. PMID: 35481648 Free PMC article. - The archaeal protein SepF is essential for cell division in Haloferax volcanii.
Nußbaum P, Gerstner M, Dingethal M, Erb C, Albers SV. Nußbaum P, et al. Nat Commun. 2021 Jun 8;12(1):3469. doi: 10.1038/s41467-021-23686-9. Nat Commun. 2021. PMID: 34103513 Free PMC article. - SepF is the FtsZ anchor in archaea, with features of an ancestral cell division system.
Pende N, Sogues A, Megrian D, Sartori-Rupp A, England P, Palabikyan H, Rittmann SKR, Graña M, Wehenkel AM, Alzari PM, Gribaldo S. Pende N, et al. Nat Commun. 2021 Jun 4;12(1):3214. doi: 10.1038/s41467-021-23099-8. Nat Commun. 2021. PMID: 34088904 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources