Microbial Community Profile and Water Quality in a Protected Area of the Caatinga Biome

The Caatinga is a semi-arid biome in northeast Brazil. The Paraguaçú River is located in the Caatinga biome, and part of its course is protected by the National Park of Chapada Diamantina (PNCD). In this study we evaluated the effect of PNCD protection on the water quality and microbial community diversity of this river by analyzing water samples obtained from points located inside and outside the PNCD in both wet and dry seasons. Results of water quality analysis showed higher levels of silicate, ammonia, particulate organic carbon, and nitrite in samples from the unprotected area compared with those from protected areas. Pyrosequencing of the 16S rRNA genes revealed that Burkholderiales was abundant in samples from all three sites during both seasons and was represented primarily by the genus Polynucleobacter and members of the Comamonadaceae family (e.g., genus Limnohabitans). During the dry season, the unprotected area showed a higher abundance of Flavobacterium sp. and Arthrobacter sp., which are frequently associated with the presence and/or degradation of arsenic and pesticide compounds. In addition, genes that appear to be related to agricultural impacts on the environment, as well as those involved in arsenic and cadmium resistance, copper homeostasis, and propanediol utilization, were detected in the unprotected areas by metagenomic sequencing. Although PNCD protection improves water quality, agricultural activities around the park may affect water quality within the park and may account for the presence of bacteria capable of pesticide degradation and assimilation, evidencing possible anthropogenic impacts on the Caatinga.     

Synthesis and degradation of fructose 2,6-bisphosphate in endosperm of castor bean seedlings

The aim of this work was to examine the possibility that fructose 2,6-bisphosphate (Fru-2,6-P₂) plays a role in the regulation of gluconeogenesis from fat. Fru-2,6-P₂ is known to inhibit cytoplasmic fructose 1,6-bisphosphatase and stimulate pyrophosphate:fructose 6-phosphate phosphotransferase from the endosperm of seedlings of castor bean (Ricinus communis). Fru-2,6-P₂ was present throughout the seven-day period in amounts from 30 to 200 picomoles per endosperm. Inhibition of gluconeogenesis by anoxia or treatment with 3-mercaptopicolinic acid doubled the amount of Fru-2,6-P₂ in detached endosperm. The maximum activities of fructose 6-phosphate,2-kinase and fructose 2,6-bisphosphatase (enzymes that synthesize and degrade Fru-2,6-P₂, respectively) were sufficient to account for the highest observed rates of Fru-2,6-P₂ metabolism. Fructose 6-phosphate,2-kinase exhibited sigmoid kinetics with respect to fructose 6-phosphate. These kinetics became hyperbolic in the presence of inorganic phosphate, which also relieved a strong inhibition of the enzyme by 3-phosphoglycerate. Fructose 2,6-bisphosphatase was inhibited by both phosphate and fructose 6-phosphate, the products of the reaction. The properties of the two enzymes suggest that in vivo the amounts of fructose-6-phosphate, 3-phosphoglycerate, and phosphate could each contribute to the control of Fru-2,6-P₂ level. Variation in the level of Fru-2,6-P₂ in response to changes in the levels of these metabolites is considered to be important in regulating flux between fructose 1,6-bisphosphate and fructose 6-phosphate during germination.     

A biochemical analysis of the effects of arachidonic acid on sarcoplasmic reticulum function

Discontinuous sucrose gradients were used to determine the degree of association between arachidonic acid and sarcoplasmic reticulum vesicle membranes. Fraction analyses showed that arachidonic acid migrated to a different region of the sucrose gradient in the presence of sarcoplasmic reticulum membranes. This could suggest that arachidonic acid was complexed into the membranes. Arrhenius curves representing the temperature dependency of Ca2+-Mg2+-ATPase activity and calcium uptake in the presence and absence of arachidonic acid were constructed. The activation energy for ATPase did not change significantly due to the presence of arachidonic acid. The curve representing control calcium uptake did not show a discontinuity. However, the curve representing calcium uptake in the presence of arachidonic acid showed discontinuities at 18 degrees C and 21 degrees C. Activation energy increased sharply between these temperatures. The results suggest that arachidonic acid reached the critical micellar concentration between these temperatures. Enthalpy decreased in the presence of arachidonic acid. This observation could suggest a transition of the protein-phospholipid complex to a less rigid state since decreased order in the membrane would decrease the energy barrier for activation of ATPase.     

Feeding patterns of elephants at the Atherstone Collaborative Nature Reserve

The African savannah elephant (Loxodonta africana Blumenbach) is a generalist herbivore that relies on widely distributed resources. Vegetation decline, aggravated by these elephants, can compromise local conservation efforts. Thus it imperative to understand the factors that drive them to consume specific plant species and plant parts. The objective of our study was to investigate the feeding patterns of African savannah elephants in the enclosed bushveld savannah at the Atherstone Collaborative Nature Reserve in South Africa. For 1 year, we examined elephant selection of woody versus herbaceous vegetation, and identified which plant species and parts were preferentially consumed. We accomplished this by directly observing feeding elephants, and by utilizing data collected on elephant footprints, dung piles, stripped bark and broken branches. We further conducted vegetation surveys to determine selection frequency relative to species abundance. Elephants showed a preference for different plant parts consumption in the feeding plots. In total, leaves, branches and bark contributed mostly to their diet. Seasonal selection patterns showed an increasing proportion of bark and branch consumption during the dry season.     

Possible risk posed by drift of the insect growth regulator pyriproxyfen to the rare dung beetle Circellium bacchus (F.) in a national park

Aerial drift of the juvenile hormone analogue (JHA), pyriproxyfen (Nemesis 100 ec®), used to control red scale on citrus on farms close to the Addo Elephant National Park in South Africa, was suspected of causing a decline in a population of the rare dung beetle species Circellium bacchus (F.) in the Park. The effect of pyriproxyfen on fertility and egg viability, as well as larval, pupal and callow adult development of C. bacchus was studied in a laboratory assay. Adult beetles, soil surface and the initial dung supply were exposed to pyriproxyfen applied as a spray at 10 times less than the concentration used commercially to simulate spray drift. Exposure of adult beetles to pyriproxyfen did not affect egg production or the viability of eggs, nor did the compound have adverse effects on immature development, indicating that pyriproxyfen is unlikely to be the cause of the observed population depression of C. bacchus.     

Maltose metabolism by pea chloroplasts

The aim of this work was to investigate the origin of maltose formed during starch breakdown in the dark by chloroplasts of Pisum sativum. The maximum catalytic activities of maltose phosphorylase and maltase in pea leaves were shown to be low, relative to those of enzymes known to be involved in starch breakdown. Fractionation of pea leaves indicated that the chloroplasts lack maltase but have enough maltose phosphorylase to synthesize the amounts of maltose formed when isolated chloroplasts breakdown starch. The absence of exogenous phosphate markedly reduced starch breakdown and maltose accumulation by isolated chloroplasts. When [¹⁴C]glucose was supplied to chloroplasts that were breaking down starch in the dark, maltose was labelled and most of the label was in the glucose moeity. It is suggested that maltose phosphorylase, using glucose-1-phosphate formed from starch by α-glucan phosphorylase, is responsible for, at least some of, the synthesis of maltose during starch breakdown by pea chloroplasts in vitro.