Misfolded plant virus proteins: elicitors and targets of ubiquitylation

Jockusch H, Wiegand C (2003)
FEBS LETTERS 545(2-3): 229-232.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Mutant tobacco mosaic virus (TMV) coat proteins (CPs) with known amino acid replacements provide well defined examples of destabilized tertiary structures. Here we show that misfolded TMV CPs, but not functional wild-type CPs, induce massive ubiquitylation in tobacco cells and that denatured, insoluble CP subunits are the main substrates of ubiquitin conjugation. As TMV CPs can be easily manipulated they are unique tools to study the molecular basis of the plant cell's response to aberrant protein structures and the associated intracellular stress reactions. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Stichworte
temperature-sensitive; mutation; insoluble protein; denaturation; coat protein; ubiquitin; tobacco mosaic virus
Erscheinungsjahr
2003
Zeitschriftentitel
FEBS LETTERS
Band
545
Ausgabe
2-3
Seite(n)
229-232
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1611205

Zitieren

Jockusch H, Wiegand C. Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS LETTERS. 2003;545(2-3):229-232.
Jockusch, H., & Wiegand, C. (2003). Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS LETTERS, 545(2-3), 229-232. https://doi.org/10.1016/S0014-5793(03)00549-0
Jockusch, Harald, and Wiegand, C. 2003. “Misfolded plant virus proteins: elicitors and targets of ubiquitylation”. FEBS LETTERS 545 (2-3): 229-232.
Jockusch, H., and Wiegand, C. (2003). Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS LETTERS 545, 229-232.
Jockusch, H., & Wiegand, C., 2003. Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS LETTERS, 545(2-3), p 229-232.
H. Jockusch and C. Wiegand, “Misfolded plant virus proteins: elicitors and targets of ubiquitylation”, FEBS LETTERS, vol. 545, 2003, pp. 229-232.
Jockusch, H., Wiegand, C.: Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS LETTERS. 545, 229-232 (2003).
Jockusch, Harald, and Wiegand, C. “Misfolded plant virus proteins: elicitors and targets of ubiquitylation”. FEBS LETTERS 545.2-3 (2003): 229-232.

8 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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The ubiquitin/26S proteasome system in plant-pathogen interactions: a never-ending hide-and-seek game.
Dielen AS, Badaoui S, Candresse T, German-Retana S., Mol Plant Pathol 11(2), 2010
PMID: 20447278
The cytosolic protein response as a subcomponent of the wider heat shock response in Arabidopsis.
Sugio A, Dreos R, Aparicio F, Maule AJ., Plant Cell 21(2), 2009
PMID: 19244141
Proteasomal degradation in plant-pathogen interactions.
Citovsky V, Zaltsman A, Kozlovsky SV, Gafni Y, Krichevsky A., Semin Cell Dev Biol 20(9), 2009
PMID: 19505586
HC-Pro protein of Potato virus Y can interact with three Arabidopsis 20S proteasome subunits in planta.
Jin Y, Ma D, Dong J, Jin J, Li D, Deng C, Wang T., J Virol 81(23), 2007
PMID: 17898064
Tobacco mosaic virus: a model system for plant biology.
Scholthof KB., Annu Rev Phytopathol 42(), 2004
PMID: 15283658

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