Activation of a plant invertase by inorganic phosphate

Activation by orthophosphate of a plant invertase from root nodules of Lupinus luteus L. has been demonstrated. The activation affects an increase in maximum velocity (V(max)) of the reaction. Activation was also achieved with a number of similar anions and it has been possible to infer a broad classification of anions capable of serving as activators. The possibility of orthophosphate activation in vivo has been considered, and there is some evidence to suggest that this could regulate invertase activity under physiological conditions.     

Species abundances influence the net biodiversity effect in mixtures of two plant species

Species abundances (evenness or identity of the dominant species in mixtures) usually are not rigorously controlled when testing relationships between plant production and species richness and may be highly dynamic in disturbed or early successional communities. Changes in species abundances may affect the yield of mixtures relative to yields expected from species monocultures [the net biodiversity effect (NBE)] by changing how species that differ in function are distributed in the plant community. To test the prediction that variation in species abundances affects the NBE via changes in the expression of functional differences among species (the complementarity effect), we grew perennial grasses and forbs in field plots in central Texas, USA, as equal-density monocultures and two-species mixtures in which relative abundances of species were varied. Function should differ more consistently between species of different growth forms than of the same growth form. We predicted, therefore, that the complementarity effect and influence of species abundances on the NBE would be more pronounced in grass/forb mixtures than in mixtures with species of the same growth form (grass/grass and forb/forb mixtures). The NBE varied with species evenness in two of the six species pairs studied and with identity of the dominant species in a third species combination. The NBE was sensitive to species proportions in both grass/grass and grass/forb assemblages. In all combinations in which the NBE differed with either evenness or identity of the dominant species, the variation resulted largely from change in the complementarity effect. Our results suggest that the NBE of mixtures is sensitive to effects of species ratios on complementarity.     

Activation of the food mutagens IQ and MeIQ by hepatic S9 fractions derived from various species

The ability of hepatic S9 mixes derived from different rodent species (rat, mouse, Syrian and Chinese hamster) to activate the mutagens 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) and 2-amino-3,4-dimethylimidazo[4,5-f]quinoline (MeIQ) was investigated using Salmonella typhimurium strain TA98. In general, the mutagenicity of IQ and MeIQ was greatest in the presence of S9 fractions from Swiss albino mice and least from fractions derived from Chinese hamsters. However, treatment of rats or hamsters with Aroclor 1254 had little or no effect on the activation of IQ or MeIQ to mutagens.     

Activation status-coupled transient S acylation determines membrane partitioning of a plant Rho-related GTPase

ROPs or RACs are plant Rho-related GTPases implicated in the regulation of a multitude of signaling pathways that function at the plasma membrane by virtue of posttranslational lipid modifications. The relationship between ROP activation status and membrane localization has not been established. Here we demonstrate that endogenous ROPs, as well as a transgenic His₆-green fluorescent protein (GFP)-AtROP6 fusion protein, were partitioned between Triton X-100-soluble and -insoluble membranes. In contrast, an activated His₆-GFP-Atrop6^CA mutant protein accumulated exclusively in detergent-resistant membranes. GDP induced accumulation of ROPs in Triton-soluble membranes, whereas GTPγS induced accumulation of ROPs in detergent-resistant membranes. Recombinant wild-type and constitutively active AtROP6 isoforms were purified from Arabidopsis plants, and their lipids were cleaved and analyzed by gas chromatography-coupled mass spectrometry. In Triton-soluble membranes, wild-type AtROP6 was only prenylated, primarily by geranylgeranyl. The activated AtROP6 that accumulated in detergent-resistant membranes was modified by prenyl and acyl lipids. The acyl lipids were identified as palmitic and stearic acids. In agreement, activated His₆-GFP-Atrop6^CAmS¹⁵⁶ in which cysteine¹⁵⁶ was mutated into serine accumulated in Triton-soluble membranes. These findings show that upon GTP binding and activation, AtROP6 and possibly other ROPs are transiently S acylated, which induces their partitioning into detergent-resistant membranes.     

Root CEC determinations to establish root biomasses of two plant species grown in mixtures

Summary The use of measurements on the cation exchange capacity (CEC) of roots in competition experiments with two plant species is suggested. If the root-CEC differences between the two species are not too small, measurement of this parameter offers a very simple way to determine the separate contributions of the two plant species in the total root biomass of the mixture. This root-CEC method can be applied to total root yields as well as to detailed root-zone studies.Grassland Species Research Group, Publication no. 48     

Activation of macrophage promatrix metalloproteinase-9 by lipopolysaccharide-associated proteinases

LPS induces an up-regulation of promatrix metalloproteinase-9 (proMMP9) gene expression in cells of the monocyte/macrophage lineage. We demonstrate here that LPS preparations are also able to activate proMMP9 made by human macrophages or THP-1 cells via LPS-associated proteinases, which cleave the N-terminal propeptide at a site or sites close to the one cleaved upon activation with organomercurial compounds. LPS-associated proteinases are serine proteinases that are able to cleave denatured collagens (gelatin) and the mammalian serine proteinase inhibitor, alpha(1)-proteinase inhibitor, thereby pushing the balance of extracellular matrix turnover even further toward degradation. A low molecular mass, low affinity inhibitor of MMP9, possibly derived from the propeptide, is generated during proMMP9 activation. However, inhibition of the LPS-associated proteinases had no effect on proMMP9 synthesis, indicating that their proteolytic activity was not required for signaling the up-regulation of the proMMP9 gene.     

Activation of higher plant phosphoenolpyruvate carboxylases by glucose-6-phosphate

Studies of the response of phosphoenolpyruvate carboxylase from C₃ (wheat [Triticum aestivum L.]), C₄ (maize [Zea mays L.]), and Crassulacean acid metabolism (CAM) (Crassula) leaves to the activator glucose-6-phosphate as a function of pH showed that the binding of the activator and the response path to activation were essentially identical for all three enzymes. The level of affinity for the activator differed, with the CAM enzyme having the highest affinity and the maize enzyme the lowest. The observed pK values suggest that histidine and cysteine groups may be involved in activation by glucose-6-phosphate. The presence of glucose-6-phosphate protected the enzyme against inactivation of the activation response by p-chloromercuribenzoate. The maximal activation response to glucose-6-phosphate showed differences among the three enzymes including different pH optima and different pH profiles. Here the maize leaf enzyme showed a potential response about twice as great as that of the C₃ and CAM enzymes.     

Activation of carcinogenic N-nitrosopropylamines to mutagens by lung and pancreas S9 fractions from various animal species and man

The mutagenic potential of 7 carcinogenic N-nitrosopropylamines was examined by the Ames liquid incubation assay, using lung and pancreas 9000 × g supernatant (S9) fractions from rats, hamsters, mice, rabbits, monkeys and humans for metabolic activation. N-Nitroso(2-hydroxypropyl)(2-oxopropyl)amine (HPOP), N-nitrosobis(2-oxopropyl)amine (BOP) and N-nitrosomethyl(2-oxopropyl)amine (MOP) showed positive mutagenicity in strain TA100 in the presence of lung S9 from each of the uninduced animals and humans. Besides the 3 N-nitrosopropylamines, N-nitrosomethyl(2-hydroxypropyl)amine (MHP) was also positive in the presence of lung S9 from polychlorinated biphenyl (PCB)-induced rats, hamsters and mice. On the other hand, in the presence of pancreas S9 from uninduced or PCB-induced animals, only HPOP and BOP showed positive mutagenicity. In contrast, N-nitrosobis(2-hydroxypropyl)amine (BHP), N-nitrosobis (2-acetoxypropyl)amine (BAP) and N-nitroso-2,6-dimethylmorpholine (NDMM) showed negative mutagenicity in the presence of lung and pancreas S9 from either uninduced or PCB-induced animals and humans. HPOP was a direct-acting mutagen, and lung and pancreas S9 from 5 animal species and man did not affect the activity. BOP was mutagenic even in the presence of bovine serum albumin. The mutagenic activation of MHP by lung S9 from PCB-induced rats, hamsters and mice was completely inhibited by preincubation in an atmosphere of carbon monoxide or by addition of cytochrome c or metyrapone to the S9 mixture, whereas 7,8-benzoflavone totally lacked this effect. However, that of MOP was insensitive to these inhibitors. These results of mutagenicity assay indicate that only the methyl derivatives of N-nitrosopropylamines, MHP and MOP are activated by the lung from 5 animal species and man, whereas the pancreas from all the tested animals did not activate the 7 N-nitrosopropylamines to mutagens, and that the phenobarbital-inducible major cytochrome P-450 in the lung of rodents is involved in the mutagenic activation of MHP.     

植物对环境应力刺激的生物学效应

植物生长在自然环境中由于其“不动性”而不可避免地要受到各种环境应力的刺激,应力－生长关系一直是生物学家和物理学家所关心的课题,是生物力学的灵魂。很多研究已经表明外界应力作用对植物的生长发育有着重要的影响。本综述了国内外关于应力对植物组织所引起的生物学效应,首先论述了环境应力所引起的宏观生物学效应,随后重点论述了环境应力所引起的生物学效应在细胞和分子水平上的研究,其中包括单个细胞的加载、电磁场、微     

Activation of RXR–PPAR heterodimers by organotin environmental endocrine disruptors

The nuclear receptor retinoid X receptor‐α (RXR‐α)–peroxisome proliferator‐activated receptor‐γ (PPAR‐γ) heterodimer was recently reported to have a crucial function in mediating the deleterious effects of organotin compounds, which are ubiquitous environmental contaminants. However, because organotins are unrelated to known RXR‐α and PPAR‐γ ligands, the mechanism by which these compounds bind to and activate the RXR‐α–PPAR‐γ heterodimer at nanomolar concentrations has remained elusive. Here, we show that tributyltin (TBT) activates all three RXR–PPAR‐α, ‐γ, ‐δ heterodimers, primarily through its interaction with RXR. In addition, the 1.9 Å resolution structure of the RXR‐α ligand‐binding domain in complex with TBT shows a covalent bond between the tin atom and residue Cys 432 of helix H11. This interaction largely accounts for the high binding affinity of TBT, which only partly occupies the RXR‐α ligand‐binding pocket. Our data allow an understanding of the binding and activation properties of the various organotins and suggest a mechanism by which these tin compounds could affect other nuclear receptor signalling pathways.