Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin

Strepp, R.; Scholz, Sirkka; Kruse, Sven; Speth, Volker; Reski, Ralf

doi:10.1073/pnas.95.8.4368

Cited by 355 publications

(297 citation statements)

References 31 publications

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“…FtsZ is a tubulin-related protein (Erickson, 1997) that polymerizes at midcell, forming a ring that shrinks until division is completed (Rothfield and Justice, 1997). Involvement of FtsZ homologs in plastid division has been clearly established in Arabidopsis (AtFtsZ1-1 and AtFtsZ2-1) and the moss Physcomitrella patens (Osteryoung et al, 1998;Strepp et al, 1998;McAndrews et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

An Arabidopsis Homolog of the Bacterial Cell Division Inhibitor SulA Is Involved in Plastid Division[W]

et al. 2004

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Plastids have evolved from an endosymbiosis between a cyanobacterial symbiont and a eukaryotic host cell. Their division is mediated both by proteins of the host cell and conserved bacterial division proteins. Here, we identified a new component of the plastid division machinery, Arabidopsis thaliana SulA. Disruption of its cyanobacterial homolog (SSulA) in Synechocystis and overexpression of an AtSulA-green fluorescent protein fusion in Arabidopsis demonstrate that these genes are involved in cell and plastid division, respectively. Overexpression of AtSulA inhibits plastid division in planta but rescues plastid division defects caused by overexpression of AtFtsZ1-1 and AtFtsZ2-1, demonstrating that its role in plastid division may involve an interaction with AtFtsZ1-1 and AtFtsZ2-1.

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Section: Introductionmentioning

confidence: 99%

An Arabidopsis Homolog of the Bacterial Cell Division Inhibitor SulA Is Involved in Plastid Division[W]

et al. 2004

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“…Since 1994, there have been seven reports of highly efficient gene targeting in P. patens, Kammerer & Cove, 1996 ;Schaefer & Zry$ d, 1997 ;Girke et al, 1998 ;Strepp et al, 1998 ;Girod et al, 1999 ;Hofmann et al, 1999). In three cases, gene targeting resulted in the generation of mutants with a null phenotype (gene knockout), thereby allowing functions to be assigned to the targeted genes and their products (Girke et al, 1998 ;Strepp et al, 1998 ;Girod et al, 1999). In all these studies, stable transformants were produced in which the transgenic DNA had been inserted into the genome of the moss, usually at a single locus and often in a concatemeric form.…”

Section: mentioning

confidence: 99%

The bryophyte Physcomitrella patens replicates extrachromosomal transgenic elements

et al. 2000

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Physcomitrella patens, recently renamed Aphanoregma patens, has been transformed with the plasmid, pBI426. On selective medium approx. 30% of regenerants expressed the transformed phenotype transiently (transients). The remaining 70% (transformants) retained their transformed phenotype (GUS-positive and resistant to G418) indefinitely when subcultured repeatedly on selective medium. However, most lost this phenotype after one or two passages through nonselective medium (unstable transformants). Approximately 0n2% of transformants retained their transformed phenotype after numerous passages through nonselective medium (stable transformants). Using PCR methodology, it has been shown that loss of the transformed phenotype by unstable transformants is invariably accompanied by disappearance of the transgenic DNA. Southern blot analysis data argue strongly that unstable transformants cultured under selective conditions contain unintegrated pBI426 as circular concatenates consisting of 3-40 copies of the plasmid. Under selective conditions, it appears that replication and\or partitioning of these extrachromosomal concatemers might be growth rate-limiting. This is the first report of a transgenic, autonomously replicating extrachromosomal element in a photosynthetic plant. A single copy of pBI426 has been inserted into the moss genome in each of three stable transformants analysed.

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“…Disruption of ftsZ in the moss Physcomitrella patens (Strepp et al, 1998) and antisense repression of FtsZ in Arabidopsis produced giant chloroplasts in each cell. Plant nuclear genes encoding FtsZ also have been identified in Chlorophyta (Osteryoung and Vierling, 1995;Strepp et al, 1998;Gaikwad et al, 2000;Mori and Tanaka, 2000), Rhodophyta (Takahara et al, , 2000a(Takahara et al, , 2000b, and Chromophyta (Fraunholz et al, 1998;Beech et al, 2000), and most of them are highly conserved compared with their cyanobacterial counterparts. Arabidopsis FtsZ (AtFtsZ1-1) and pea FtsZ (Gaikwad et al, 2000) were imported into chloroplasts in vitro.…”

Section: Introductionmentioning

confidence: 99%

“…In addition to morphological studies, molecular genetic studies show that plastid division requires nucleus-encoded homologs of FtsZ (Osteryoung and Vierling, 1995;Strepp et al, 1998), a protein that forms a cytokinetic ring in bacteria beneath the plasma membrane (Bi and Lutkenhaus, 1991;reviewed in Bramhill, 1997). Disruption of ftsZ in the moss Physcomitrella patens (Strepp et al, 1998) and antisense repression of FtsZ in Arabidopsis produced giant chloroplasts in each cell.…”

Section: Introductionmentioning

confidence: 99%

Novel Filaments 5 nm in Diameter Constitute the Cytosolic Ring of the Plastid Division Apparatus

Miyagishima¹,

Takahara²,

Kuroiwa³

2001

The Plant Cell

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The plastid division apparatus (called the plastid-dividing ring) has been detected in several plant and algal species at the constricted region of plastids by transmission electron microscopy. The apparatus is composed of two or three rings: an outer ring in the cytosol, an inner ring in the stroma, and a middle ring in the intermembrane space. The components of these rings are not clear. FtsZ, which forms the bacterial cytokinetic ring, has been proposed as a component of both the inner and outer rings. Here, we present the ultrastructure of the outer ring at high resolution. To visualize the outer ring by negative staining, we isolated dividing chloroplasts from a synchronized culture of a red alga, Cyanidioschyzon merolae , and lysed them with nonionic detergent Nonidet P-40. Nonidet P-40 extracted primarily stroma, thylakoids, and the inner and middle rings, leaving the envelope and outer ring largely intact. Negative staining revealed that the outer ring consists of a bundle of 5-nm filaments in which globular proteins are spaced 4.8 nm apart. Immunoblotting using an FtsZ-specific antibody failed to show immunoreactivity in the fraction containing the filament. Moreover, the filament structure and properties are unlike those of known cytoskeletal filaments. The bundle of filaments forms a very rigid structure and does not disassemble in 2 M urea. We also identified a dividing phase-specific 56-kD protein of chloroplasts as a candidate component of the ring. Our results suggest that the main architecture of the outer ring did not descend from cyanobacteria during the course of endosymbiosis but was added by the host cell early in plant evolution. INTRODUCTIONEukaryotic cells contain organelles that are duplicated and inherited by daughter cells during cell division. Among these organelles, mitochondria and plastids are unique in that they contain DNA-protein complexes (nucleoids) and machinery sufficient for protein synthesis. It is generally believed that mitochondria and plastids arose from prokaryotic endosymbionts during eukaryotic evolution. The endosymbiotic theory states that the progenitor of mitochondria was an ␣ -proteobacterium and that the plastid ancestor was a cyanobacterium (Gray, 1992). Mitochondria and plastids multiply by the division of preexisting organelles, as do bacteria (Leech et al., 1981;Kuroiwa, 1982Kuroiwa, , 1991Possingham and Lawrence, 1983; Boffey and Lloyd, 1988). Of the characterized mitochondrial and plastid genomes, however, none has a complete set of genes sufficient for self-replication. Mitochondria that cannot synthesize proteins as a result of large genome deletions (petite mutant) (Attardi and Schatz, 1988) and plastids that lack ribosomes (Hashimoto and Possingham, 1989) still can proliferate. Therefore, it is believed that products from the host (nuclear) genomes perform mitochondrial and plastid division. Nuclear regulation of organelle division remains poorly understood, but in plastid division both the plastid-dividing ring (PD ring) (summarized in Kuroiwa et ...

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Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin

Cited by 355 publications

References 31 publications

An Arabidopsis Homolog of the Bacterial Cell Division Inhibitor SulA Is Involved in Plastid Division[W]

An Arabidopsis Homolog of the Bacterial Cell Division Inhibitor SulA Is Involved in Plastid Division[W]

The bryophyte Physcomitrella patens replicates extrachromosomal transgenic elements

Novel Filaments 5 nm in Diameter Constitute the Cytosolic Ring of the Plastid Division Apparatus

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