An evaluation of the Cypress Creek watershed for inorganic chemical load as it flows into Lake Houston

Background. The Cypress Creek is one of the main tributaries of Lake Houston, which provides drinking water to 21.4 million customers. Furthermore, the watershed is being utilized for contact and non-contact recreation, such as canoeing, swimming, hiking trail, and picnics. Water along the creek is impacted by numerous wastewater outfalls from both point and non-point sources. As the creek flows into Lake Houston, it carries both organic and inorganic contaminants that may affect the drinking water quality of this important water source reservoir. Objective. This study was carried out to evaluate the inorganic chemical load of the water in Cypress Creek along its entire length, from the headwaters in Waller County and up to the drainage into Lake Houston. The purpose was to determine whether there are hazardous concentrations of metals in the water and what would be the likely sources. Method. Samples were collected at 29 sites along the creek and analyzed for 29 metals, 17 of which were on the Environmental Protection Agency priority pollution list. Public access sites primarily at bridges were used for sample collection. Samples were transported on ice to the University Of Texas School Of Public Health laboratory, spiked with 2 ml HNO3 kept overnight in the refrigerator, and the following day transported to the EPA laboratory for analysis. Analysis was done by EPA Method 200.7-ICP, Method 200.8ICP/MS and Method 245.1-CVAAS. Results. Metals were present above the detection limits at 65% of sites. Concentrations of aluminum, iron, sodium, potassium, magnesium, and calcium, were particularly high at all sites. Aluminum, sodium, and iron concentrations greatly exceeded the EPA secondary drinking water standards at all sites. ^ Conclusion. The recreational water along Cypress Creek is impacted by wastewater from both permitted and non-permitted outfalls, which deposit inorganic substances into the water. Although a number of inorganic contaminants were present in the water, toxic metals regulated by the EPA were mostly below the recommended limits. However, high concentrations of aluminum, sodium, and iron in the Cypress Creek bring forward the issue of unauthorized discharges of salt water from mining, as well as industrial and domestic wastewater.^

Plasticity of lipid-protein interactions in the function and topogenesis of the membrane protein lactose permease from Escherichia coli.

Phosphatidylcholine (PC) has been widely used in place of naturally occurring phosphatidylethanolamine (PE) in reconstitution of bacterial membrane proteins. However, PC does not support native structure or function for several reconstituted transport proteins. Lactose permease (LacY) of Escherichia coli, when reconstituted in E. coli phospholipids, exhibits energy-dependent uphill and energy-independent downhill transport function and proper conformation of periplasmic domain P7, which is tightly linked to uphill transport function. LacY expressed in cells lacking PE and containing only anionic phospholipids exhibits only downhill transport and lacks native P7 conformation. Reconstitution of LacY in the presence of E. coli-derived PE, but not dioleoyl-PC, results in uphill transport. We now show that LacY exhibits uphill transport and native conformation of P7 when expressed in a mutant of E. coli in which PC completely replaces PE even though the structure is not completely native. E. coli-derived PC and synthetic PC species containing at least one saturated fatty acid also support the native conformation of P7 dependent on the presence of anionic phospholipids. Our results demonstrate that the different effects of PE and PC species on LacY structure and function cannot be explained by differences in the direct interaction of the lipid head groups with specific amino acid residues alone but are due to more complex effects of the physical and chemical properties of the lipid environment on protein structure. This conclusion is supported by the effect of different lipids on the proper folding of domain P7, which indirectly influences uphill transport function.

Developmental Changes in the Structure and Composition of the Postsynaptic Density

The development of the brain and its underlying circuitry is dependent on the formation of trillions of chemical synapses, which are highly specialized contacts that regulate the flow of information from one neuron to the next. It is through these synaptic connections that neurons wire together into networks capable of performing specific tasks, and activity-dependent changes in their structural and physiological state is one way that the brain is thought to adapt and store information. At the ultrastructural level, developmental and activity-dependent changes in the size and shape of dendritic spines have been well documented, and it is widely believed that structural changes in spines are a hallmark sign of synapse maturation and alteration of synaptic physiology. While changes in spine structure have been studied extensively, changes in one of its most prominent components, the postsynaptic density (PSD), have largely evaded observation. The PSD is a protein-rich organelle on the cytoplasmic side of the postsynaptic membrane, where it sits in direct opposition to the presynaptic terminal. The PSD functions both to cluster neurotransmitter receptors at the cell surface as well as organize the intracellular signaling molecules responsible for transducing extracellular signals to the postsynaptic cell. Much is known about the chemical composition of the PSD, but the structural arrangement of its molecular components is not well documented. Adding to the difficulty of understanding such a complex mass of protein machinery is the fact that its protein composition is known to change in response to synaptic activity, meaning that its structure is plastic and no two PSDs are identical. Here, immuno-gold labeling and electron tomography of PSDs isolated throughout development was used to track changes in both the structure and molecular composition of the PSD. State-of-the-art cryo-electron tomography was used to study the fine structure of the PSD during development, and provides an unprecedented glimpse into its molecular architecture in an un-fixed, unstained and hydrated state. Through this analysis, large structural and compositional changes are apparent and suggest a model by which the PSD is first assembled as a mesh-like lattice of proteins that function as support for the later recruitment of various PSD components. Spatial analysis of the recruitment of proteins into the PSD demonstrated that its assembly has an underlying order.