Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Autor Nach Häufigkeit alphabetisch sortiert: Monostori, T
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C
Autor Nach Häufigkeit alphabetisch sortiert: Maucher, H
Autor Nach Häufigkeit alphabetisch sortiert: Gray, W.M.
Autor Nach Häufigkeit alphabetisch sortiert: Verbeek, M.
Autor Nach Häufigkeit alphabetisch sortiert: Strehmel, N.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Proc Natl Acad Sci USA
Autor Nach Häufigkeit alphabetisch sortiert: Krüler, V.
Autor Nach Häufigkeit alphabetisch sortiert: Schulze-Lefert, P.
Autor Nach Häufigkeit alphabetisch sortiert: Flores, R.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Sci Rep
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Viruses
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Trends Plant Sci.
Autor Nach Häufigkeit alphabetisch sortiert: Kühn, H.
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (2)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- 0 (7)
- Nucleic Acids Res. (3)
- FEBS Lett. (2)
- J. Gen. Virol. (2)
- Proc. Natl. Acad. Sci. U.S.A. (2)
- RNA Biol. (2)
- Annu. Rev. Microbiol. (1)
- BBA-Mol. Cell Biol. Lipids (1)
- BIOspektrum (1)
- Biology of Plant-Microbe Interactions (1)
- EMBO J. (1)
- Eur. J. Biochem. (1)
- Int. J. Mol. Sci. (1)
- J. Biol. Chem. (1)
- J. Exp. Bot. (1)
- PLOS ONE (1)
- PLOS Pathog. (1)
- Plant Cell (1)
- Plant Viruses (1)
- Planta (1)
- RNA (1)
- RNA Technologies (1)
- Sci. Rep. (1)
- Science (1)
- Trends Plant Sci. (1)
- Virology (1)
- Viruses (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Wasternack, C. (5)
- Abel, S. (3)
- Calderón Villalobos, L. I. A. (1)
- Carbonell, A. (1)
- Daròs, J.-A. (1)
- De la Peña, M. (1)
- Delker, C. (1)
- Dinesh, D. C. (1)
- Feussner, I. (1)
- Flores, R. (1)
- Gago, S. (1)
- Gas, M.-E. (1)
- Grubb, C. D. (1)
- Hause, B. (1)
- Kühn, H. (1)
- Molina-Serrano, D. (1)
- Nohales, M.-?. (1)
- Parthier, B. (1)
- Quint, M. (1)
- Ticconi, C. A. (1)
Zeige Ergebnisse 1 bis 2 von 2.
Flores, R.; Gas, M.-E.; Molina-Serrano, D.; Nohales, M.-?.; Carbonell, A.; Gago, S.; De la Peña, M.; Daròs, J.-A.; Viroid Replication: Rolling-Circles, Enzymes and Ribozymes Viruses 1, 317-334, (2009) DOI: 10.3390/v1020317
Viroids, due to their small size and lack of protein-coding capacity, must rely essentially on their hosts for replication. Intriguingly, viroids have evolved the ability to replicate in two cellular organella, the nucleus (family Pospiviroidae) and the chloroplast (family Avsunviroidae). Viroid replication proceeds through an RNA-based rolling-circle mechanism with three steps that, with some variations, operate in both polarity strands: i) synthesis of longer-than-unit strands catalyzed by either the nuclear RNA polymerase II or a nuclear-encoded chloroplastic RNA polymerase, in both instances redirected to transcribe RNA templates, ii) cleavage to unit-length, which in the family Avsunviroidae is mediated by hammerhead ribozymes embedded in both polarity strands, while in the family Pospiviroidae the oligomeric RNAs provide the proper conformation but not the catalytic activity, and iii) circularization. The host RNA polymerases, most likely assisted by additional host proteins, start transcription from specific sites, thus implying the existence of viroid promoters. Cleavage and ligation in the family Pospiviroidae is probably catalyzed by an RNase III-like enzyme and an RNA ligase able to circularize the resulting 5’ and 3’ termini. Whether a chloroplastic RNA ligase mediates circularization in the family Avsunviroidae, or this reaction is autocatalytic, remains an open issue.
Feussner, I.; Kühn, H.; Wasternack, C.; Lipoxygenase-dependent degradation of storage lipids Trends Plant Sci. 6, 268-273, (2001) DOI: 10.1016/S1360-1385(01)01950-1
Oilseed germination is characterized by the mobilization of storage lipids as a carbon source for the germinating seedling. In spite of the importance of lipid mobilization, its mechanism is only partially understood. Recent data suggest that a novel degradation mechanism is initiated by a 13-lipoxygenase during germination, using esterified fatty acids specifically as substrates. This 13-lipoxygenase reaction leads to a transient accumulation of ester lipid hydroperoxides in the storage lipids, and the corresponding oxygenated fatty acid moieties are preferentially removed by specific lipases. The free hydroperoxy fatty acids are subsequently reduced to their hydroxy derivatives, which might in turn undergo β-oxidation.