High impact information on Papaver

• Identification of residues in a hydrophilic loop of the Papaver rhoeas S protein that play a crucial role in recognition of incompatible pollen [1].
• We have constructed mutant derivatives of the S1 protein from Papaver rhoeas by using site-directed mutagenesis and have tested their biological activity [1].
• A potential signaling role for profilin in pollen of Papaver rhoeas [2].
• The roles of latex and the vascular bundle in morphine biosynthesis in the opium poppy, Papaver somniferum [3].
• Two early and potential rate-limiting steps in the biosynthesis of isoquinoline alkaloids, such as morphine and codeine, in opium poppy (Papaver somniferum) involve decarboxylation of L-tyrosine and L-dihydroxyphenylalanine (L-dopa) to yield tyramine and dopamine, respectively [4].

Biological context of Papaver

• Transformation of opium poppy (Papaver somniferum L.) with antisense berberine bridge enzyme gene (anti-bbe) via somatic embryogenesis results in an altered ratio of alkaloids in latex but not in roots [5].
• Furthermore, changes in morphology correlated to cell viability and enzyme release in those cultures treated with papaver, 4'-OH and 6-OH papaverine [6].
• Duration of cell cycle, onset of S phase and induced mitotic synchronisation in seeds of opium poppy, Papaver somniferum L [7].

Anatomical context of Papaver

• Enzymic conversion of reticuline to salutaridine by cell-free systems from Papaver somniferum [8].

Associations of Papaver with chemical compounds

• In Papaver somniferum (opium poppy) and related species, (S)-reticuline serves as a branch-point intermediate in the biosynthesis of numerous isoquinoline alkaloids [9].
• S-Adenosyl-L-methionine:(R,S)-reticuline 7-O-methyltransferase converts reticuline to laudanine in tetrahydrobenzylisoquinoline biosynthesis in the opium poppy Papaver somniferum [10].
• Three key benzylisoquinoline alkaloid biosynthetic enzymes, (S)-N-methylcoclaurine-3'-hydroxylase (CYP80B1), berberine bridge enzyme (BBE), and codeinone reductase (COR), were localized in cultured opium poppy (Papaver somniferum) cells by sucrose density gradient fractionation and immunogold labeling [11].
• Here we show that a vector based on TRV sequences is effective at silencing the endogenous phytoene desaturase (PapsPDS) gene in Papaver somniferum (opium poppy) [12].
• Molecular cloning and functional expression of codeinone reductase: the penultimate enzyme in morphine biosynthesis in the opium poppy Papaver somniferum [13].

Gene context of Papaver

• Two highly homologous phospholipase D isoenzymes from Papaver somniferum L. with different transphosphatidylation potential [14].
• In Papaver rhoeas, the pollen S gene product is predicted to be a receptor that interacts with the stigmatic S protein in an S specific manner [15].
• S-protein mutants indicate a functional role for SBP in the self-incompatibility reaction of Papaver rhoeas [15].
• Self-incompatibility (SI) in Papaver rhoeas triggers a ligand-mediated signal transduction cascade, resulting in the inhibition of incompatible pollen tube growth [16].
• Molecular analysis of two functional homologues of the S3 allele of the Papaver rhoeas self-incompatibility gene isolated from different populations [17].

Analytical, diagnostic and therapeutic context of Papaver

• Characterization of proteins in latex of the opium poppy (Papaver somniferum) using two-dimensional gel electrophoresis and microsequencing [18].
• However, the administration of buthionine sulfoximine to cell cultures dramatically decreased the time by which papaver induced cellular injury (2 hr vs 8 hr) [19].

References