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Publikation

Calderon-Villalobos, L. I.; Tan, X.; Zheng, N.; Estelle, M. Auxin Perception—Structural Insights Cold Spring Harb Perspect Biol 2, a005546, (2010) DOI: 10.1101/cshperspect.a005546

The identity of the auxin receptor(s) and the mechanism of auxin perception has been a subject of intense interest since the discovery of auxin almost a century ago. The development of genetic approaches to the study of plant hormone signaling led to the discovery that auxin acts by promoting degradation of transcriptional repressors called Aux/IAA proteins. This process requires a ubiquitin protein ligase (E3) called SCFTIR1 and related SCF complexes. Surprisingly, auxin works by directly binding to TIR1, the F-box protein subunit of this SCF. Structural studies demonstrate that auxin acts like a molecular glue, to stabilize the interaction between TIR1 and the Aux/IAA substrate. These exciting results solve an old problem in plant biology and reveal new mechanisms for E3 regulation and hormone perception.
Publikation

Abel, S.; Theologis, A. Odyssey of Auxin Cold Spring Harb Perspect Biol 2, a004572, (2010) DOI: 10.1101/cshperspect.a004572

The history of plant biology is inexorably intertwined with the conception and discovery of auxin, followed by the many decades of research to comprehend its action during growth and development. Growth responses to auxin are complex and require the coordination of auxin production, transport, and perception. In this overview of past auxin research, we limit our discourse to the mechanism of auxin action. We attempt to trace the almost epic voyage from the birth of the hormonal concept in plants to the recent crystallographic studies that resolved the TIR1-auxin receptor complex, the first structural model of a plant hormone receptor. The century-long endeavor is a beautiful illustration of the power of scientific reasoning and human intuition, but it also brings to light the fact that decisive progress is made when new technologies emerge and disciplines unite.
Publikation

Calderón Villalobos, L.I.; Nill, C.; Marrocco, K.; Kretsch, T.; Schwechheimer, C. The evolutionarily conserved Arabidopsis thaliana F-box protein AtFBP7 is required for efficient translation during temperature stress Gene 392(1-2), 106-116, (2007) DOI: 10.1016/j.gene.2006.11.016

In eukaryotes, E3 ubiquitin ligases (E3s) mediate the ubiquitylation of proteins that are destined for degradation by the ubiquitin-proteasome system. In SKP1/CDC53/F-box protein (SCF)-type E3 complexes, the interchangeable F-box protein confers specificity to the E3 ligase through direct physical interactions with the degradation substrate. The vast majority of the approximately 700 F-box proteins from the plant model organism Arabidopsis thaliana remain to be characterized. Here, we investigate the previously uncharacterized and evolutionarily conserved Arabidopsis F-box protein 7 (AtFBP7), which is encoded by a unique gene in Arabidopsis (At1g21760). Several apparent fbp7 loss-of-function alleles do not have an obvious phenotype. AtFBP7 is ubiquitously expressed and its expression is induced after cold and heat stress. When following up on a reported co-purification of the eukaryotic elongation factor-2 (eEF-2) with YLR097c, the apparent budding yeast orthologue of AtFBP7, we discovered a general defect in protein biosynthesis after cold and heat stress in fbp7 mutants. Thus, our findings suggest that AtFBP7 is required for protein synthesis during temperature stress.
Publikation

Biondi, E.; Branciamore, S.; Fusi, L.; Gago, S.; Gallori, E. Catalytic activity of hammerhead ribozymes in a clay mineral environment: Implications for the RNA world. Gene 389, 10-18, (2007) DOI: 10.1016/j.gene.2006.09.002

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Publikation

Guranowski, A.; Miersch, O.; Staswick, P.E.; Suza, W.; Wasternack, C. Substrate specificity and products of side-reactions catalyzed by jasmonate:amino acid synthetase (JAR1) FEBS Letters 581, 815-820, (2007) DOI: 10.1016/j.febslet.2007.01.049

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Publikation

Flores, R.; Delgado, S.; Gas, M.E.; Carbonell, A.; Molina, D.; Gago, S.; de la Peña, M. Viroids: the minimal non-coding RNA's with autonomous replication FEBS Letters 567, 42-48, (2004)

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Publikation

Morgan, K.E.; Zarembinski, T.I.; Theologis, A.; Abel, S. Biochemical characterization of recombinant polypeptides corresponding to the predicted ßαα-fold in Aux/IAA proteins FEBS Letters 454, 283-287, (1999)

The plant hormone indoleacetic acid (IAA or auxin) transcriptionally activates a select set of early genes. The Auxl IAA class of early auxin-responsive genes encodes a large family of short-lived, nuclear proteins. Aux/IAA polypeptides homo-and heterodimerize, and interact with auxin-response transcription factors (ARFs) via C-terminal regions conserved in both protein families. This shared region contains a predicted βαα motif similar to the prokaryotic β-Ribbon DNA binding domain, which mediates both protein dimerization and DNA recognition. Here, we show by circular dichroism spectroscopy and by chemical cross-linking experiments that recombinant peptides corresponding to the predicted βαα region of three Aux/IAA proteins from Arabidopsis thaliana contain substantial α-helical secondary structure and undergo homo- and heterotypic interactions in vitro. Our results indicate a similar biochemical function of the plant βαα domain and suggest that the βαα fold plays an important role in mediating combinatorial interactions of Aux/IAA and ARF proteins to specifically regulate secondary gene expression in response to auxin.
Publikation

Bohlmann, H.; Vignutelli, A.; Hilpert, B.; Miersch, O.; Wasternack, C.; Apel, K. Wounding and chemicals induce expression of the Arabidopsis gene Thi2.1, encoding a fungal defense thionin, via the octadecanoid pathway FEBS Letters 437, 281-286, (1998)

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Publikation

Hertel, S.; Knöfel, H.-D.; Kramell, R.; Miersch, O. Partial purification and characterization of a jasmonic acid conjugate cleaving amidohydrolase from the fungus <EM>Botryodiplodia theobromae</EM> FEBS Letters 407, 105-110, (1997)

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Publikation

Görschen, E.; Dunaeva, M.; Reeh, I.; Wasternack, C. Overexpression of the jasmonate inducible 23 kDa protein (JIP 23) from barley in transgenic tobacco leads to the repression of leaf proteins FEBS Letters 419, 58-62, (1997)

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