Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and self‐assembly

Smith, Arthur A.; Johnson, Carol B.; Vitha, Stanislav; Holzenburg, Andreas

doi:10.1016/j.febslet.2009.11.044

Cited by 29 publications

(29 citation statements)

References 59 publications

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“…However, they reported that mixing FtsZ1 and FtsZ2 in equimolar reactions inhibited GTPase activity, whereas we observed a slight stimulation at 3 mM GTP and above. In assembly assays, Smith et al observed single protofilaments for individual and mixed FtsZ1 and FtsZ2, as reported for bacterial FtsZ (4,5), but indicated that the filament morphologies were unlike any observed for the bacterial proteins (23). In contrast, the morphologies of our assemblies appear more like those seen for bacterial FtsZs (e.g.…”

Section: Discussioncontrasting

confidence: 52%

“…According to the primer sequences reported by Smith et al in their supplemental methods, their proteins were truncated after amino acids 39 and 73 for FtsZ1 and FtsZ2, respectively, which would have left a portion of the predicted transit peptide on FtsZ1 and removed conserved residues from the probable mature form of FtsZ2. Further experiments will be required to understand why our findings differ from those of Smith et al (23).…”

Section: Discussioncontrasting

confidence: 46%

“…A more recent study by Smith et al (23) using Arabidopsis FtsZ1 and FtsZ2 bearing both c-Myc and His tags on their C termini indicated that both FtsZ1 and FtsZ2 are capable of GTP-dependent protofilament formation. However, the results of the latter study differed in many respects from those reported here.…”

Section: Discussionmentioning

confidence: 99%

“…These findings, along with data showing that the molar ratio between Arabidopsis FtsZ1 and FtsZ2 remains constant throughout leaf development (20), suggest that their stoichiometry is important for chloroplast division activity. In vitro, FtsZ1 and FtsZ2 have been reported to exhibit GTPase activity and to undergo GTPdependent assembly into protofilaments (21)(22)(23). However, the previous analyses have been limited in scope, and whether FtsZ1 and FtsZ2 form heteropolymers has not been investigated.…”

mentioning

confidence: 89%

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GTP-dependent Heteropolymer Formation and Bundling of Chloroplast FtsZ1 and FtsZ2

Olson

Wang

Osteryoung

2010

Journal of Biological Chemistry

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Bacteria and chloroplasts require the ring-forming cytoskeletal protein FtsZ for division. Although bacteria accomplish division with a single FtsZ, plant chloroplasts require two FtsZ types for division, FtsZ1 and FtsZ2. These proteins colocalize to a mid-plastid Z ring, but their biochemical relationship is poorly understood. We investigated the in vitro behavior of recombinant FtsZ1 and FtsZ2 separately and together. Both proteins bind and hydrolyze GTP, although GTPase activities are low compared with the activity of Escherichia coli FtsZ. Each protein undergoes GTP-dependent assembly into thin protofilaments in the presence of calcium as a stabilizing agent, similar to bacterial FtsZ. In contrast, when mixed without calcium, FtsZ1 and FtsZ2 exhibit slightly elevated GTPase activity and coassembly into extensively bundled protofilaments. Coassembly is enhanced by FtsZ1, suggesting that it promotes lateral interactions between protofilaments. Experiments with GTPase-deficient mutants reveal that FtsZ1 and FtsZ2 form heteropolymers. Maximum coassembly occurs in reactions containing equimolar FtsZ1 and FtsZ2, but significant coassembly occurs at other stoichiometries. The FtsZ1:FtsZ2 ratio in coassembled structures mirrors their input ratio, suggesting plasticity in protofilament and/or bundle composition. This behavior contrasts with that of ␣-and ␤-tubulin and the bacterial tubulin-like proteins BtubA and BtubB, which coassemble in a strict 1:1 stoichiometry. Our findings raise the possibility that plasticity in FtsZ filament composition and heteropolymerization-induced bundling could have been a driving force for the coevolution of FtsZ1 and FtsZ2 in the green lineage, perhaps arising from an enhanced capacity for the regulation of Z ring composition and activity in vivo.Cell division in bacteria and chloroplast division in plants both require FtsZ, a tubulin-like GTPase that functions as a contractile ring, the Z ring, inside the cell or chloroplast. Mutations in bacterial FtsZ genes disrupt cell division, resulting in long filamented cells (reviewed in Refs. 1-3). Purified bacterial FtsZ undergoes GTP-dependent, hydrolysis-independent polymerization primarily into single protofilaments (4, 5), but protofilament sheets and bundles form in the presence of stabilizing agents that promote lateral interactions (6 -8). Polymerization stimulates FtsZ GTPase activity because the catalytic site for GTP hydrolysis lies in the longitudinal interface between adjacent monomers within the polymer (9). GTP hydrolysis destabilizes protofilaments, leading to disassembly (10). The in vivo structure of the bacterial Z ring is not yet clear, but recent models suggest it may be built from short overlapping protofilaments that are stabilized at the division site by accessory factors (11, 12). The Z ring functions partly as a scaffold for other cell division proteins and recently has also been shown to provide contractile force for membrane constriction (13,14).In most bacteria, including the cyanobacterial relatives of chloropl...

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Section: Discussioncontrasting

confidence: 52%

Section: Discussioncontrasting

confidence: 46%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 89%

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GTP-dependent Heteropolymer Formation and Bundling of Chloroplast FtsZ1 and FtsZ2

Olson

Wang

Osteryoung

2010

Journal of Biological Chemistry

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“…Biochemically, the plant FtsZ proteins behave in a similar fashion to bacterial FtsZ where both FtsZ1 and FtsZ2 are capable of binding and hydrolysing GTP, albeit at a lower rate compared with bacterial FtsZ (Smith et al 2010;Olson et al 2010). Recently, the enzymology of the plant FtsZs and how this relates to function has been under scrutiny.…”

Section: Biochemical Characteristics Of Plastid Division Componentsmentioning

confidence: 99%

Emerging facets of plastid division regulation

Basak

Møller

2012

Planta

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Plastids are complex organelles that are integrated into the plant host cell where they diVerentiate and divide in tune with plant diVerentiation and development. In line with their prokaryotic origin, plastid division involves both evolutionary conserved proteins and proteins of eukaryotic origin where the host has acquired control over the process. The plastid division apparatus is spatially separated between the stromal and the cytosolic space but where clear coordination mechanisms exist between the two machineries. Our knowledge of the plastid division process has increased dramatically during the past decade and recent Wndings have not only shed light on plastid division enzymology and the formation of plastid division complexes but also on the integration of the division process into a multicellular context. This review summarises our current knowledge of plastid division with an emphasis on biochemical features, the functional assembly of protein complexes and regulatory features of the overall process.

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Plastid Division

Maple‐Grødem

Raynaud

2014

Plastid Biology

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Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and self‐assembly

Cited by 29 publications

References 59 publications

GTP-dependent Heteropolymer Formation and Bundling of Chloroplast FtsZ1 and FtsZ2

GTP-dependent Heteropolymer Formation and Bundling of Chloroplast FtsZ1 and FtsZ2

Emerging facets of plastid division regulation

Plastid Division

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