Omanische Heilpflanze im Fokus der Phytochemie IPB-Wissenschaftler und Partner aus Dhofar haben jüngst die omanische Heilpflanze Terminalia dhofarica unter die phytochemische Lupe genommen. Die Pflanze ist reich an…
Geschmack ist vorhersagbar: Mit FlavorMiner. FlavorMiner heißt das Tool, das IPB-Chemiker und Partner aus Kolumbien jüngst entwickelt haben. Das Programm kann, basierend auf maschinellem Lernen (KI), anhand der…
Quint, M.; Drost, H.-G.; Gabel, A.; Ullrich, K. K.; Bönn, M.; Grosse, I.;A transcriptomic hourglass in plant embryogenesisNature49098-101(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.
Publikation
Pereira, C.; Barreto Júnior, C. B.; Kuster, R. M.; Simas, N. K.; Sakuragui, C. M.; Porzel, A.; Wessjohann, L.;Flavonoids and a neolignan glucoside from Guarea macrophylla (Meliaceae)Quím. Nova351123-1126(2012)DOI: 10.1590/S0100-40422012000600010
This work describes the phytochemical study of the methanol extract obtained from leaves of Guarea macrophylla, leading to the isolation and identification of three flavonoid glycosides (quercetin 3-O-β-D-glucopyranoside, quercetin 3-O-b-D-galactopyranoside, kaempferol 7-O-β-D-glucopyranoside) and a neolignan glucoside, dehydrodiconiferyl alcohol-4-β-D-glucoside. All compounds were identified by a combination of spectroscopic methods (1H, 1D, 2D NMR, 13C and UV), ESI-MS and comparison with the literature data. This is the first report of flavonoids in the genus Guarea and of a neolignan glucoside in the Meliaceae family.
Publikation
Parthier, C.; Görlich, S.; Jaenecke, F.; Breithaupt, C.; Bräuer, U.; Fandrich, U.; Clausnitzer, D.; Wehmeier, U. F.; Böttcher, C.; Scheel, D.; Stubbs, M. T.;The O-Carbamoyltransferase TobZ Catalyzes an Ancient Enzymatic ReactionAngew. Chem. Int. Ed.514046-4052(2012)DOI: 10.1002/anie.201108896
An ancient reaction vessel: TobZ carbamoylates the antibiotic tobramycin to form nebramycin 5′. The YrdC‐like domain (blue) catalyzes the formation of the novel intermediate carbamoyladenylate, which is channeled through a common “reaction chamber” to the Kae1‐like domain (brown), site of carbamoyl transfer.
Publikation
Parthier, C.; Görlich, S.; Jaenecke, F.; Breithaupt, C.; Bräuer, U.; Fandrich, U.; Clausnitzer, D.; Wehmeier, U. F.; Böttcher, C.; Scheel, D.; Stubbs, M. T.;Die O-Carbamoyltransferase TobZ katalysiert eine enzymatische Reaktion frühen UrsprungsAngew. Chem.1244122-4128(2012)DOI: 10.1002/ange.201108896
Ein uraltes Reaktionsgefäß: TobZ carbamoyliert das Antibiotikum Tobramycin unter Bildung von Nebramycin‐5′. Dabei katalysiert die YrdC‐ähnliche Domäne (blau) die Bildung eines intermediären Carbamoyladenylats, das innerhalb einer tunnelartigen Reaktionskammer zur Kae1‐ähnlichen Domäne (braun), dem Ort des Carbamoyltransfers, transferiert wird.