Filamentous temperature-sensitive Z (FtsZ) isoforms specifically interact in the chloroplasts and in the cytosol of Physcomitrella patens.
Plant filamentous temperature-sensitive Z (FtsZ) proteins have been reported to be involved in biological processes related to plastids. However, the precise functions of distinct isoforms are still elusive. Here, the intracellular localization of the FtsZ1-1 isoform in a moss, Physcomitrella patens, was examined. Furthermore, the in vivo interaction behaviour of four distinct FtsZ isoforms was investigated. Localization studies of green fluorescent protein (GFP)-tagged FtsZ1-1 and fluorescence resonance energy transfer (FRET) analyses employing all dual combinations of four FtsZ isoforms were performed in transient protoplast transformation assays. FtsZ1-1 is localized to network structures inside the chloroplasts and exerts influence on plastid division. Interactions between FtsZ isoforms occur in distinct ordered structures in the chloroplasts as well as in the cytosol. The results expand the view of the involvement of Physcomitrella FtsZ proteins in chloroplast and cell division. It is concluded that duplication and diversification of ftsZ genes during plant evolution were the main prerequisites for the successful remodelling and integration of the prokaryotic FtsZ-dependent division mechanism into the cellular machineries of distinct complex processes in plants.
Gremillon
Louis
L
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
Kiessling
Justine
J
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
Hause
Bettina
B
Leibniz Institute of Plant Biochemistry, Department of Secondary Metabolism, Weinberg 3, 06120 Halle/Saale, Germany.
Decker
Eva L
EL
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
Reski
Ralf
R
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
Sarnighausen
Eric
E
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
D029681:Arabidopsis Proteins; D001426:Bacterial Proteins / Q000378:metabolism; D019068:Bryopsida / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D002455:Cell Division; D002736:Chloroplasts / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism* / Q000648:ultrastructure; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D049452:Green Fluorescent Proteins / Q000032:analysis; D010940:Plant Proteins / Q000032:analysis / Q000378:metabolism*; D025941:Protein Interaction Mapping; D020033:Protein Isoforms / Q000032:analysis / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000032:analysis
D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C095113:FTSZ protein, Arabidopsis; C071525:FtsZ protein, Bacteria; D010940:Plant Proteins; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins