Cell cycle-dependent modulation of FtsZ expression in synchronized tobacco BY2 cells

El-Shami, Mahmoud; El-Kafafi, S.; Falconet, Denis; Lerbs-Mache, Silva

doi:10.1007/s00438-002-0660-y

Cited by 31 publications

(13 citation statements)

References 39 publications

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“…Only FtsZ1 is able to polymerize in vitro and forms GTP-dependent rod-shaped polymers and rings similar to the bacterial structures, but FtsZ2 can promote GTP-independent FtsZ1 polymerization. These data together with other results showing the interaction of only FtsZ2 with ARC6 and an earlier expression of FtsZ2 during the cell cycle in BY2 cells [18] suggests that FtsZ2 and FtsZ1 fulfil different functions during chloroplast division [19].…”

Section: While Most Bacteria (Including Cyanobacteria) Have Only One supporting

confidence: 77%

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Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana

El-Kafafi

Karamoko

Pignot-Paintrand

et al. 2007

Biochemical Journal

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FtsZ is a key protein involved in bacterial and organellar division. Bacteria have only one ftsZ gene, while chlorophytes (higher plants and green alga) have two distinct FtsZ gene families, named FtsZ1 and FtsZ2. This raises the question of why chloroplasts in these organisms need distinct FtsZ proteins to divide. In order to unravel new functions associated with FtsZ proteins, we have identified and characterized an Arabidopsis thaliana FtsZ1 loss-of-function mutant. ftsZ1-knockout mutants are impeded in chloroplast division, and division is restored when FtsZ1 is expressed at a low level. FtsZ1-overexpressing plants show a drastic inhibition of chloroplast division. Chloroplast morphology is altered in ftsZ1, with chloroplasts having abnormalities in the thylakoid membrane network. Overexpression of FtsZ1 also induced defects in thylakoid organization with an increased network of twisting thylakoids and larger grana. We show that FtsZ1, in addition to being present in the stroma, is tightly associated with the thylakoid fraction. This association is developmentally regulated since FtsZ1 is found in the thylakoid fraction of young developing plant leaves but not in mature and old plant leaves. Our results suggest that plastid division protein FtsZ1 may have a function during leaf development in thylakoid organization, thus highlighting new functions for green plastid FtsZ.

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Section: While Most Bacteria (Including Cyanobacteria) Have Only One supporting

confidence: 77%

“…The conserved Nterminal sequence is sufficient for bacterial FtsZ polymerization [17]. The major difference between FtsZ1 and FtsZ2 in higher plants concerns a single amino acid change in the conserved "tubulin signature motif" [18].…”

Section: While Most Bacteria (Including Cyanobacteria) Have Only One mentioning

confidence: 99%

Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana

El-Kafafi

Karamoko

Pignot-Paintrand

et al. 2007

Biochemical Journal

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“…Both proteins reside in the stromal compartment of the chloroplast and localize to rings at the plastid division site (21–23). The two most noted differences between the FtsZ1 and FtsZ2 proteins are (a) the variability of a single amino acid residue in the otherwise conserved ‘tubulin signature motif’ (24) and (b) the conservation in FtsZ2 proteins, but not FtsZ1, of a short C‐terminal motif found in most bacterial FtsZ proteins. In E. coli , this motif mediates an interaction between FtsZ and two membrane‐associated Z‐ring stabilizing factors, FtsA and ZipA (25–27).…”

Section: Ftsz and Control Of Z‐ring Assembly And Placementmentioning

confidence: 99%

Chloroplast Division

Glynn

Miyagishima

Yoder

et al. 2007

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105

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Chloroplasts are descendants of cyanobacteria and divide by binary fission. Several components of the division apparatus have been identified in the past several years and we are beginning to appreciate the plastid division process at a mechanistic level. In this review, we attempt to summarize the most recent developments in the field and assemble these observations into a working model of plastid division in plants. Plastids: Characteristics, Origins and DistributionWithout chloroplasts, plant and animal life would not exist. Plastids have been studied most extensively with regard to their role in photosynthesis, and are essential to the plant itself, being required for a select of amino acid and lipid metabolism, assimilation of nitrogen and sulfur into organic compounds, signaling in response to environmental cues and biosynthesis of plant hormones (1)(2)(3)(4)(5). Despite all we have learned over the past century regarding this organelle, we still know relatively little about its replication-which, superficially, seems a simple process of binary fission. Because plastid division and biogenesis are an integral part of plant growth and development, understanding of the division process is paramount to our understanding of plant and organelle biology.Plastids arose from an endosymbiotic relationship between a primitive biciliate protozoan and an ancient cyanobacterium that began 1.2-1.5 billion years ago (Figure 1) (6,7). Initially, each partner derived some mutual benefit: the cyanobacterium occupied and exploited an untapped protective niche and the host extracted reduced carbon and other nutrients from its new tenant. Time, selective pressure and mutation bring us to the present day where the chloroplast is a prisoner in its own home, having lost more than 90% of the gene content present in its free-living ancestor. Most of the plastid division genes identified to date are cyanobacterial in origin and encode division proteins localized inside the organelle. These are directed to the plastid post-translationally by N-terminal transit peptides that are cleaved upon import. A few components of the division complex were invented by the host after endosymbiosis and function on the surface of the organelle in contact with the cytosol; the mechanisms targeting these proteins to the chloroplast surface are unknown. In land plants, all known plastid division genes reside in the nucleus-none are found in the plastid genome-although in at least one unicellular green alga two plastid division genes remain associated with the plastid genome (8).The terms chloroplast and plastid are often used interchangeably, but in vascular plants chloroplasts are actually a subset of plastids, each of which is specialized for a given set of functions within a specific cell type. All plastids are surrounded by two envelope membranes and are derived by division from a population of proplastids within the meristematic (stem) cells of the plant. Beyond land plants, red algae, green algae and diatoms also contain plastids. Even apicomplex...

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“…It also lost the ability to freely replicate, because the complete protein set for division is encoded in the nucleus (Hashimoto and Possingham, 1989; Kuroiwa et al, 1998). Furthermore, cell- and plastid-divisions are synchronized (El-Shami et al, 2002; Raynaud et al, 2005), although it can be uncoupled to a certain degree, as demonstrated by several mutant lines defective in plastid division (Pyke and Leech, 1992; Osteryoung et al, 1998; Asano et al, 2004; Raynaud et al, 2004). …”

Section: Introductionmentioning

confidence: 99%

The plastid outer envelope – a highly dynamic interface between plastid and cytoplasm

Breuers¹

2011

Front. Plant Sci.

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Plastids are the defining organelles of all photosynthetic eukaryotes. They are the site of photosynthesis and of a large number of other essential metabolic pathways, such as fatty acid and amino acid biosyntheses, sulfur and nitrogen assimilation, and aromatic and terpenoid compound production, to mention only a few examples. The metabolism of plastids is heavily intertwined and connected with that of the surrounding cytosol, thus causing massive traffic of metabolic precursors, intermediates, and products. Two layers of biological membranes that are called the inner (IE) and the outer (OE) plastid envelope membranes bound the plastids of Archaeplastida. While the IE is generally accepted as the osmo-regulatory barrier between cytosol and stroma, the OE was considered to represent an unspecific molecular sieve, permeable for molecules of up to 10 kDa. However, after the discovery of small substrate specific pores in the OE, this view has come under scrutiny. In addition to controlling metabolic fluxes between plastid and cytosol, the OE is also crucial for protein import into the chloroplast. It contains the receptors and translocation channel of the TOC complex that is required for the canonical post-translational import of nuclear-encoded, plastid-targeted proteins. Further, the OE is a metabolically active compartment of the chloroplast, being involved in, e.g., fatty acid metabolism and membrane lipid production. Also, recent findings hint on the OE as a defense platform against several biotic and abiotic stress conditions, such as cold acclimation, freezing tolerance, and phosphate deprivation. Moreover, dynamic non-covalent interactions between the OE and the endomembrane system are thought to play important roles in lipid and non-canonical protein trafficking between plastid and endoplasmic reticulum. While proteomics and bioinformatics has provided us with comprehensive but still incomplete information on proteins localized in the plastid IE, the stroma, and the thylakoids, our knowledge of the protein composition of the plastid OE is far from complete. In this article, we report on the recent progress in discovering novel OE proteins to draw a conclusive picture of the OE. A “parts list” of the plastid OE will be presented, using data generated by proteomics of plastids isolated from various plant sources.

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Cell cycle-dependent modulation of FtsZ expression in synchronized tobacco BY2 cells

Cited by 31 publications

References 39 publications

Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana

Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana

Chloroplast Division

The plastid outer envelope – a highly dynamic interface between plastid and cytoplasm

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