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Publikationen - Molekulare Signalverarbeitung

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Publikation

Guseman, J. M.; Hellmuth, A.; Lanctot, A.; Feldman, T. P.; Moss, B. L.; Klavins, E.; Calderón Villalobos, L. I. A.; Nemhauser, J. L. Auxin-induced degradation dynamics set the pace for lateral root development Development 142, 1-5, (2015) DOI: 10.1242/dev.117234

Auxin elicits diverse cell behaviors through a simple nuclear signaling pathway initiated by degradation of Aux/IAA co-repressors. Our previous work revealed that members of the large Arabidopsis Aux/IAA family exhibit a range of degradation rates in synthetic contexts. However, it remained an unresolved issue whether differences in Aux/IAA turnover rates played a significant role in plant responses to auxin. Here, we use the well-established model of lateral root development to directly test the hypothesis that the rate of auxin-induced Aux/IAA turnover sets the pace for auxin-regulated developmental events. We did this by generating transgenic plants expressing degradation rate variants of IAA14, a crucial determinant of lateral root initiation. Progression through the well-established stages of lateral root development was strongly correlated with the engineered rates of IAA14 turnover, leading to the conclusion that Aux/IAAs are auxin-initiated timers that synchronize developmental transitions
Publikation

Bürstenbinder, K.; Savchenko, T.; Müller, J.; Adamson, A.W.; Stamm, G.; Kwong, R.; Zipp, B.J.; Dhurvas Chandrasekaran, D. & Abel, S. Arabidopsis calmodulin-binding protein IQ67-domain 1 localizes to microtubules and interacts with kinesin light chain-related protein-1 J Biol Chem 288, 1871-1882, (2013) DOI: 10.1074/jbc.M112.396200

Calcium (Ca2+) is a key second messenger in eukaryotes and regulates diverse cellular processes, most notably via calmodulin (CaM). In Arabidopsis thaliana, IQD1 (IQ67 domain 1) is the founding member of the IQD family of putative CaM targets. The 33 predicted IQD proteins share a conserved domain of 67 amino acids that is characterized by a unique arrangement of multiple CaM recruitment motifs, including so-called IQ motifs. Whereas IQD1 has been implicated in the regulation of defense metabolism, the biochemical functions of IQD proteins remain to be elucidated. In this study we show that IQD1 binds to multiple Arabidopsis CaM and CaM-like (CML) proteins in vitro and in yeast two-hybrid interaction assays. CaM overlay assays revealed moderate affinity of IQD1 to CaM2 (Kd ∼ 0.6 μm). Deletion mapping of IQD1 demonstrated the importance of the IQ67 domain for CaM2 binding in vitro, which is corroborated by interaction of the shortest IQD member, IQD20, with Arabidopsis CaM/CMLs in yeast. A genetic screen of a cDNA library identified Arabidopsis kinesin light chain-related protein-1 (KLCR1) as an IQD1 interactor. The subcellular localization of GFP-tagged IQD1 proteins to microtubules and the cell nucleus in transiently and stably transformed plant tissues (tobacco leaves and Arabidopsis seedlings) suggests direct interaction of IQD1 and KLCR1 in planta that is supported by GFP∼IQD1-dependent recruitment of RFP∼KLCR1 and RFP∼CaM2 to microtubules. Collectively, the prospect arises that IQD1 and related proteins provide Ca2+/CaM-regulated scaffolds for facilitating cellular transport of specific cargo along microtubular tracks via kinesin motor proteins.
Publikation

Ziegler, J.; Brandt, W.; Geißler, R.; Facchini, P. J. Removal of Substrate Inhibition and Increase in Maximal Velocity in the Short Chain Dehydrogenase/Reductase Salutaridine Reductase Involved in Morphine Biosynthesis J Biol Chem 284, 26758-26767, (2009) DOI: 10.1074/jbc.M109.030957

Salutaridine reductase (SalR, EC 1.1.1.248) catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine. It belongs to a new, plant-specific class of short-chain dehydrogenases, which are characterized by their monomeric nature and increased length compared with related enzymes. Homology modeling and substrate docking suggested that additional amino acids form a novel -helical element, which is involved in substrate binding. Site-directed mutagenesis and subsequent studies on enzyme kinetics revealed the importance of three residues in this element for substrate binding. Further replacement of eight additional residues led to the characterization of the entire substrate binding pocket. In addition, a specific role in salutaridine binding by either hydrogen bond formation or hydrophobic interactions was assigned to each amino acid. Substrate docking alsorevealed an alternative mode for salutaridine binding, which could explain the strong substrate inhibition of SalR. An alternate arrangement of salutaridine in the enzyme was corroborated by the effect of various amino acid substitutions on substrate inhibition. In most cases, the complete removal of substrate inhibition was accompanied by a substantial loss in enzyme activity. However, some mutations greatly reduced substrate inhibition while maintaining or even increasing the maximal velocity. Based on these results, a double mutant of SalRwas created that exhibited the complete absence of substrate inhibition and higher activity compared with wild-type SalR.
Publikation

Wasternack, C. Jasmonates: An update on biosynthesis, signal transduction and action in plant stress response, growth and development Annals of Botany 100, 681-697, (2007) DOI: 10.1093/aob/mcm079

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Publikation

Schilling, S.; Stenzel, I.; von Bohlen, A.; Wermann, M.; Schulz, K.; Demuth, H.-U.; Wasternack, C. Isolation and characterization of the glutaminyl cyclases from Solanum tuberosum and Arabidopsis thaliana: implications for physiological functions Biol. Chem 388, 145-153, (2007) DOI: 10.1515/BC.2007.016

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Bücher und Buchkapitel

Stumpe, M.; Stenzel, I.; Weichert, H.; Hause, B.; Feussner, I. The lipoxygenase pathway in mycorrhizal roots of <span>Medicago truncatula</span> (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers, Dordrecht 287-290, (2003)

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Bücher und Buchkapitel

Ziegler, J.; Hamberg, M.; Miersch, O. Allene oxide cyclase from corn: Partial purification and characterization (Williams, J.P., Mobashsher, U., Khan, M.U., Lem, N.W.). Kluwer Academic Publishers, Dordrecht 99-101, (1997)

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Bücher und Buchkapitel

Feussner, I.; Kühn, H.; Wasternack, C. Do Lipoxygenases initiate ß-oxidation? (Williams, J.P., Mobashsher, U., Khan, M.U. & Lem, N.W.). Kluwer Academic Publishers, Dordrecht 250-252, (1997)

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