Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Field Crop Res
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: J. Plant Physiol
Typ der Publikation: Publikation
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Int J Mol Sci
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biochemistry
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Curr Opin Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Meth Enzymol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Nature
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (3)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- Plant Physiol. (29)
- Plant J. (28)
- Phytochemistry (21)
- Planta (13)
- FEBS Lett. (12)
- Plant Cell (12)
- J. Exp. Bot. (11)
- PLOS ONE (10)
- New Phytol. (9)
- Proc. Natl. Acad. Sci. U.S.A. (9)
- Trends Plant Sci. (9)
- J. Biol. Chem. (8)
- Curr. Biol. (7)
- Front. Plant Sci. (7)
- J. Plant Physiol. (7)
- Plant Cell Physiol. (7)
- Curr. Opin. Plant Biol. (6)
- BMC Plant Biol. (5)
- Biol. Chem. (5)
- Nat. Plants (5)
- Plant Growth Regul. (5)
- Plant Signal Behav. (5)
- Theor. Appl. Genet. (5)
- J. Plant Growth Regul. (4)
- Nat. Commun. (4)
- Nucleic Acids Res. (4)
- Ann. Bot. (3)
- Bot. Acta (3)
- EMBO J. (3)
- Int. J. Mol. Sci. (3)
- Mol. Plant (3)
- Nat. Chem. Biol. (3)
- Physiol. Plant. (3)
- Plant Mol. Biol. (3)
- Virus Res. (3)
- eLife (3)
- ACS Chem. Biol. (2)
- Amino Acids (2)
- Anal. Biochem. (2)
- Annu. Rev. Plant Biol. (2)
- BMC Biol. (2)
- Bio Protoc. (2)
- Biochem. Soc. Trans. (2)
- Biologie in unserer Zeit (2)
- Chromatographia (2)
- Cold Spring Harb. Perspect. Biol. (2)
- Fett/Lipid (2)
- Gene (2)
- Genetika (2)
- J. Chromatogr. A (2)
- J. Gen. Virol. (2)
- Mol. Biol. Evol. (2)
- Nature (2)
- New Biotechnol. (2)
- PLOS Pathog. (2)
- Plant Biol. (2)
- Plant Cell Environ. (2)
- Plant Sci. (2)
- Plants (2)
- RNA Biol. (2)
- Sci. Rep. (2)
- Science (2)
- Seed Sci. Res. (2)
- Virology (2)
- Acta Biol. Szeged. (1)
- Acta Physiol. Plant. (1)
- Annu. Rev. Microbiol. (1)
- Annu. Rev. Phytopathol. (1)
- AoB PLANTS (1)
- Arch. Virol. (1)
- Autophagy (1)
- BBA-Mol. Cell Biol. Lipids (1)
- BIOspektrum (1)
- BMC Evol. Biol. (1)
- BMC Genomics (1)
- BioEssays (1)
- Biocell (1)
- Biochem. J. (1)
- Biochemistry (1)
- Biochimie (1)
- Biologia (1)
- Biotechnol. Adv. (1)
- Biotechnol. Lett. (1)
- Braz. J. Plant Physiol. (1)
- Bull. Environ. Contam. Toxicol. (1)
- Cell (1)
- Cell Rep. (1)
- Cereal Res. Commun. (1)
- ChemBioChem (1)
- Curr. Opin. Biotech. (1)
- Cytoskeleton (1)
- Dev. Cell (1)
- Development (1)
- Drugs Exp. Clin. Res. (1)
- Ecotoxicol. Environ. Saf. (1)
- Electron. J. Biotechnol. (1)
- Environ. Exp. Bot. (1)
- Environ. Sci. Pollut. Res. (1)
- Equine Vet. Educ. (1)
- Equine Vet. J. (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Bönn, M. (1)
- Calderon-Villalobos, L. I. A. (1)
- Demuth, H.-U. (1)
- Drost, H.-G. (1)
- Estelle, M. (1)
- Gabel, A. (1)
- Grosse, I. (1)
- Hoffmann, T. (1)
- Manhart, S. (1)
- Quint, M. (1)
- Robinson, C. V. (1)
- Rosche, F. (1)
- Schilling, S. (1)
- Sharon, M. (1)
- Tan, X. (1)
- Ullrich, K. K. (1)
- Wasternack, C. (1)
- Zheng, C. (1)
- Zheng, N. (1)
Zeige Ergebnisse 1 bis 3 von 3.
Quint, M.; Drost, H.-G.; Gabel, A.; Ullrich, K. K.; Bönn, M.; Grosse, I.; A transcriptomic hourglass in plant embryogenesis Nature 490, 98-101, (2012) DOI: 10.1038/nature11394
Animal and plant development starts with a constituting phase called embryogenesis, which evolved independently in both lineages1. Comparative anatomy of vertebrate development—based on the Meckel-Serrès law2 and von Baer’s laws of embryology3 from the early nineteenth century—shows that embryos from various taxa appear different in early stages, converge to a similar form during mid-embryogenesis, and again diverge in later stages. This morphogenetic series is known as the embryonic ‘hourglass’4,5, and its bottleneck of high conservation in mid-embryogenesis is referred to as the phylotypic stage6. Recent analyses in zebrafish and Drosophila embryos provided convincing molecular support for the hourglass model, because during the phylotypic stage the transcriptome was dominated by ancient genes7 and global gene expression profiles were reported to be most conserved8. Although extensively explored in animals, an embryonic hourglass has not been reported in plants, which represent the second major kingdom in the tree of life that evolved embryogenesis. Here we provide phylotranscriptomic evidence for a molecular embryonic hourglass in Arabidopsis thaliana, using two complementary approaches. This is particularly significant because the possible absence of an hourglass based on morphological features in plants suggests that morphological and molecular patterns might be uncoupled. Together with the reported developmental hourglass patterns in animals, these findings indicate convergent evolution of the molecular hourglass and a conserved logic of embryogenesis across kingdoms.
Tan, X.; Calderon-Villalobos, L. I. A.; Sharon, M.; Zheng, C.; Robinson, C. V.; Estelle, M.; Zheng, N.; Mechanism of auxin perception by the TIR1 ubiquitin ligase Nature 446, 640-645, (2007) DOI: 10.1038/nature05731
Auxin is a pivotal plant hormone that controls many aspects of plant growth and development. Perceived by a small family of F-box proteins including transport inhibitor response 1 (TIR1), auxin regulates gene expression by promoting SCF ubiquitin-ligase-catalysed degradation of the Aux/IAA transcription repressors, but how the TIR1 F-box protein senses and becomes activated by auxin remains unclear. Here we present the crystal structures of the Arabidopsis TIR1–ASK1 complex, free and in complexes with three different auxin compounds and an Aux/IAA substrate peptide. These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket. Anchored to the base of the TIR1 pocket, auxin binds to a partially promiscuous site, which can also accommodate various auxin analogues. Docked on top of auxin, the Aux/IAA substrate peptide occupies the rest of the TIR1 pocket and completely encloses the hormone-binding site. By filling in a hydrophobic cavity at the protein interface, auxin enhances the TIR1–substrate interactions by acting as a ‘molecular glue’. Our results establish the first structural model of a plant hormone receptor.
Schilling, S.; Hoffmann, T.; Rosche, F.; Manhart, S.; Wasternack, C.; Demuth, H.-U.; Heterologous Expression and Characterization of Human Glutaminyl Cyclase: Evidence for a Disulfide Bond with Importance for Catalytic Activity Biochemistry 41, 10849-10857, (2002) DOI: 10.1021/bi0260381
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of pyroglutamate residues from glutamine at the N-terminus of peptides and proteins. In the current study, human QC was functionally expressed in the secretory pathway of Pichia pastoris, yielding milligram quantities after purification from the supernatant of a 5 L fermentation. Initial characterization studies of the recombinant QC using MALDI-TOF mass spectrometry revealed correct proteolytic processing and N-glycosylation at both potential sites with similar 2 kDa extensions. CD spectral analysis indicated a high α-helical content, which contrasts with plant QC from Carica papaya. The kinetic parameters for conversion of H-Gln-Tyr-Ala-OH by recombinant human QC were almost identical to those previously reported for purified bovine pituitary QC. However, the results obtained for conversion of H-Gln-Gln-OH, H-Gln-NH2, and H-Gln-AMC were found to be contradictory to previous studies on human QC expressed intracellularly in E. coli. Expression of QC in E. coli showed that approximately 50% of the protein did not contain a disulfide bond that is present in the entire QC expressed in P. pastoris. Further, the enzyme was consistently inactivated by treatment with 15 mM DTT, whereas deglycosylation had no effect on enzymatic activity. Analysis of the fluorescence spectra of the native, reduced, and unfolded human QC point to a conformational change of the protein upon treatment with DTT. In terms of the different enzymatic properties, the consequences of QC expression in different environments are discussed.