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  • Article

    Conservative sorting in the muroplasts of Cyanophora paradoxa : a reevaluation based on the completed genome sequence

    Steiner, Jürgen, Bhattacharya, Debashish, Löffelhardt, Wolfgang
    Symbiosis, 2012, Vol.58(1), pp.127-133 [Revue évaluée par les pairs]
    Springer Science & Business Media B.V.
    Titre: Conservative sorting in the muroplasts of Cyanophora paradoxa : a reevaluation based on the completed genome sequence
    Auteur: Steiner, Jürgen; Bhattacharya, Debashish; Löffelhardt, Wolfgang
    Sujet: Cyanophora paradoxa - Glaucophyta - Muroplasts - Conservative sorting
    Description: After primary endosymbiosis, massive gene transfer occurred from the genome of the cyanobacterial endosymbiont to the nucleus of the protist host cell. In parallel, a specific protein import apparatus arose for reimport of many, but not all products of the genes moved to the nuclear genome. Presequences evolved to allow recognition of plastid proteins at the envelope and their translocation to the stroma. However, plastids (and cyanobacteria) also comprise five other subcompartments. Protein sorting to the cyanobacterial thylakoid membrane, the thylakoid lumen, the inner envelope membrane, the periplasmic space, and the outer envelope membrane is achieved by prokaryotic protein translocases recognizing, e.g., signal sequences. The “conservative sorting” hypothesis postulates that these translocases remained functional in endosymbiotic organelles and obtained their passengers not only from imported proteins but also from proteins synthesized in organello . For proteins synthesized in the cytosol, a collaboration of the general import apparatus and the former prokaryotic translocase is necessary which is often reflected by the use of bipartite presequences, e.g., stroma targeting peptide and signal peptide. For plants, this concept has been experimentally proven and verified. The muroplasts from Cyanophora paradoxa , that have several features more in common with cyanobacteria than with plastids, were analyzed with the availability of the recently completed nuclear genome sequence. Interesting findings include the absence of the post-translational signal recognition particle pathway, dual Sec translocases in thylakoid and inner envelope membranes that are produced from a single set of genes, and a co-translational signal recognition pathway operating without a 4.5S RNA component.
    Fait partie de: Symbiosis, 2012, Vol.58(1), pp.127-133
    Identifiant: 0334-5114 (ISSN); 1878-7665 (E-ISSN); 10.1007/s13199-012-0203-1 (DOI)

  • Film

    Demenz & [und] Esprit : Jürgen Steiner im Gespräch mit Helga Rohra und Richard Taylor

    Steiner, Jürgen, Rohra, Helga, Taylor, Richard, Benz, Ulrike
    Interkantonale Hochschule für Heilpädagogik (Zürich)
    Zürich : HfH
    Recherche de la disponibilité
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    Titre: Demenz & [und] Esprit [Enregistrement vidéo] : Jürgen Steiner im Gespräch mit Helga Rohra und Richard Taylor / Prod.: Interkantonale Hochschule für Heilpädagogik Zürich ; Regie, Schnitt & Postprod.: Ulrike Benz
    Auteur: Steiner, Jürgen; Rohra, Helga; Taylor, Richard; Benz, Ulrike
    Contributeur: Interkantonale Hochschule für Heilpädagogik (Zürich)
    Editeur: Zürich : HfH
    Date: 2013
    Collation: 1 DVD-Video (45 Min.) + 1 Booklet
    Collection: HfH DVD
    Documents dans cette collection: HfH DVD
    Sujet RERO: Démence - [Entretiens] - [DVD]
    Note: Sprache: Englisch, ohne Untertitel
    Classification: vs-heso DVD-537
    No RERO: R007680459

  • Plusieurs versions

    CyberKnife radiosurgery leading to long-lasting complete remission in locally relapsed solitary plasmacytoma of the bone

    Theiler, Georg, Schwetz, Verena, Gstettner, Christian, Wowra, Berndt, Fürweger, Christoph, Steiner, Juergen, Schmidt, Helmut
    Annals of Hematology, 2015, Vol.94(7), pp.1251-1253 [Revue évaluée par les pairs]

  • Plusieurs versions

    Identification of protein N-termini in Cyanophora paradoxa cyanelles: transit peptide composition and sequence determinants for precursor maturation

    Köhler, Daniel, Dobritzsch, Dirk, Hoehenwarter, Wolfgang, Helm, Stefan, Steiner, Jürgen M, Baginsky, Sacha
    Frontiers in plant science, 2015, Vol.6, pp.559 [Revue évaluée par les pairs]

  • Plusieurs versions

    Secondary Aortic Dissection after Endoluminal Treatment of an Intramural Hematoma of the Thoracoabdominal Aorta: Endovascular Extension with Two Stent Grafts and Scarce Distal Landing

    Kalmar, Peter I, Oberwalder, Peter, Schedlbauer, Peter, Steiner, Jürgen, Portugaller, Rupert H
    Case Reports in Medicine, 2013, Vol.2013, 4 pages [Revue évaluée par les pairs]

  • Plusieurs versions

    A Possible Role for Short Introns in the Acquisition of Stroma-Targeting Peptides in the Flagellate Euglena gracilis

    Vesteg, Matej, Vacula, Rostislav, Steiner, Jürgen M, Mateášiková, Bianka, Löffelhardt, Wolfgang, Brejová, Bro&Ncaron, A, Kraj&Ccaron, Ovi&Ccaron, , Juraj
    DNA Research, 2010, Vol. 17(4), pp.223-231 [Revue évaluée par les pairs]

  • Plusieurs versions

    Evolutionary conservation of dual Sec translocases in the cyanelles of Cyanophora paradoxa

    Löffelhardt Wolfgang, Steiner Jürgen M, Yusa Fumie
    BMC Evolutionary Biology, 01 November 2008, Vol.8(1), p.304 [Revue évaluée par les pairs]

  • Article

    Homologous protein import machineries in chloroplasts and cyanelles

    Steiner, Jürgen M, Yusa, Fumie, Pompe, Johannes A, Löffelhardt, Wolfgang
    The Plant journal : for cell and molecular biology, November 2005, Vol.44(4), pp.646-52 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
    Titre: Homologous protein import machineries in chloroplasts and cyanelles
    Auteur: Steiner, Jürgen M; Yusa, Fumie; Pompe, Johannes A; Löffelhardt, Wolfgang
    Sujet: Algal Proteins -- Metabolism; Cyanophora -- Metabolism
    Description: The cyanelles of the glaucocystophyte alga Cyanophora paradoxa resemble endosymbiotic cyanobacteria, especially in the presence of a peptidoglycan wall between the inner and outer envelope membranes. However, it is now clear that cyanelles are in fact primitive plastids. Phylogenetic analyses of plastid, nuclear and mitochondrial genes support a single primary endosymbiotic event. In this scenario, cyanelles and all other plastid types are derived from an ancestral photosynthetic organelle combining the high gene content of rhodoplasts and the peptidoglycan wall of cyanelles. This means that the import apparatuses of all primary plastids, i.e. those from glaucocystophytes, red algae, green algae and higher plants, should be homologous. If this is the case, then transit sequences should be similar and heterologous import experiments feasible. Thus far, heterologous in vitro import has been shown in one direction only: precursors from C. paradoxa were imported into isolated pea or spinach chloroplasts. Cyanelle transit sequences differ from chloroplast stroma targeting peptides in containing in their N-terminal domain an invariant phenylalanine residue which is shown here to be crucial for import. In addition, we now demonstrate that heterologous precursors are readily imported into isolated cyanelles, provided that the essential phenylalanine residue is engineered into the N-terminal part of chloroplast transit peptides. The cyanelle and likely also the rhodoplast import apparatus can be envisaged as prototypes with a single receptor/channel showing this requirement for N-terminal phenylalanine. In chloroplasts, multiple receptors with overlapping and less stringent specificities have evolved, explaining the efficient heterologous import of native precursors from C. paradoxa.
    Fait partie de: The Plant journal : for cell and molecular biology, November 2005, Vol.44(4), pp.646-52
    Identifiant: 0960-7412 (ISSN); 16262713 Version (PMID)

  • Plusieurs versions

    The invariant phenylalanine of precursor proteins discloses the importance of Omp85 for protein translocation into cyanelles

    Schleiff Enrico, Löffelhardt Wolfgang, Martin Roman, Wunder Tobias, Steiner Jürgen M
    BMC Evolutionary Biology, 01 November 2007, Vol.7(1), p.236 [Revue évaluée par les pairs]
    Directory of Open Access Journals (DOAJ)
  • Plusieurs versions

    Characterization of apcC , the nuclear gene for the phycobilisome core linker polypeptide L c 7.8 from the glaucocystophyte alga Cyanophora paradoxa . Import of the precursor into isolated cyanelles and integration of the mature protein into intact phycobilisomes

    Steiner, Jürgen, Pompe, Johannes, Löffelhardt, Wolfgang
    Current Genetics, 2003, Vol.44(3), pp.132-137 [Revue évaluée par les pairs]