Physicochemical assessment and bacteriological studies of hand-dug wells of major markets in south western, Nigeria

Rapid population in developing nations has imposed stress on groundwater resources, thus the need to assess physicochemical and bacteriological impact of microbes on hand-dug wells along some major markets in Ibadan Southwestern Nigeria. Water samples from hand-dug wells were measured sequentially, and total dissolved solute (TDS), pH, electrical conductivity (EC), salinity, and temperature were measured in situ. Water samples were analyzed at a Microbiology Laboratory. Most probable techniques used for micro-organism analysis were in three stages: presumptive test used for confirmation of Escherichia coli, confirmed test for total viable bacteria count (TVBC), and complete test to reconfirm the presence of coliform. Presumptive test showed high rate of E. coli in most of the hand-dug wells with (37.5 %). Confirmed test revealed Staphylococcus aureus to be 25 %, followed by Proteus vulgaris (14.6 %), Bacillus species (12.5 %), Pseudomonas aeruginosa (8.3 %), and Klebsiella spp. (2.1 %) respectively. Total viable bacteria counts are 500 to 192,000. Physicochemical results (total dissolved solute (TDS), pH, electrical conductivity (EC), salinity, temperature) when compared with WHO (2006) and SON (2007) revealed all the parameters to be within the permissible limits except pH (5.8 to 9.56), and high values of the parameters were caused by organic matter. High E. coli in the study area revealed influence of human and animal fecal that coul

The Human TPR Protein TTC4 Is a Putative Hsp90 Co-Chaperone Which Interacts with CDC6 and Shows Alterations in Transformed Cells

BACKGROUND: The human TTC4 protein is a TPR (tetratricopeptide repeat) motif-containing protein. The gene was originally identified as being localized in a genomic region linked to breast cancer and subsequent studies on melanoma cell lines revealed point mutations in the TTC4 protein that may be associated with the progression of malignant melanoma. METHODOLOGY/PRINCIPLE FINDINGS: Here we show that TTC4 is a nucleoplasmic protein which interacts with HSP90 and HSP70, and also with the replication protein CDC6. It has significant structural and functional similarities with a previously characterised Drosophila protein Dpit47. We show that TTC4 protein levels are raised in malignant melanoma cell lines compared to melanocytes. We also see increased TTC4 expression in a variety of tumour lines derived from other tissues. In addition we show that TTC4 proteins bearing some of the mutations previously identified from patient samples lose their interaction with the CDC6 protein. CONCLUSIONS/SIGNIFICANCE: Based on these results and our previous work with the Drosophila Dpit47 protein we suggest that TTC4 is an HSP90 co-chaperone protein which forms a link between HSP90 chaperone activity and DNA replication. We further suggest that the loss of the interaction with CDC6 or with additional client proteins could provide one route through which TTC4 could influence malignant development of cells

Hsp70 chaperones: Cellular functions and molecular mechanism

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100

Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast

Plasmodium falciparum causes the most virulent form of malaria and encodes a large number of molecular chaperones. Because the parasite encounters radically different environments during its lifecycle, many members of this chaperone ensemble may be essential for P. falciparum survival. Therefore, Plasmodium chaperones represent novel therapeutic targets, but to establish the mechanism of action of any developed therapeutics, it is critical to ascertain the functions of these chaperones. To this end, we report the development of a yeast expression system for PfHsp70-1, a P. falciparum cytoplasmic chaperone. We found that PfHsp70-1 repairs mutant growth phenotypes in yeast strains lacking the two primary cytosolic Hsp70s, SSA1 and SSA2, and in strains harboring a temperature sensitive SSA1 allele. PfHsp70-1 also supported chaperone-dependent processes such as protein translocation and ER associated degradation, and ameliorated the toxic effects of oxidative stress. By introducing engineered forms of PfHsp70-1 into the mutant strains, we discovered that rescue requires PfHsp70-1 ATPase activity. Together, we conclude that yeast can be co-opted to rapidly uncover specific cellular activities mediated by malarial chaperones. © 2011 Bell et al

Global changes of extreme coastal wave energy fluxes triggered by intensified teleconnection patterns

In this study we conducted a comprehensive modeling analysis to identify global trends in extreme wave energy flux (WEF) along coastlines in the 21st century under a high emission pathway (Representative Concentration Pathways 8.5). For the end of the century, results show a significant increase up to 30% in 100 year return level WEF for the majority of the coastal areas of the southern temperate zone, while in the Northern Hemisphere large coastal areas are characterized by a significant negative trend. We show that the most significant long-term trends of extreme WEF can be explained by intensification of teleconnection patterns such as the Antarctic Oscillation, El Niño–Southern Oscillation, and North Atlantic Oscillation. The projected changes will have broad implications for ocean engineering applications and disaster risk management. Especially low-lying coastal countries in the Southern Hemisphere will be particularly vulnerable due to the combined effects of projected relative sea level rise and more extreme wave activities

Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)

Malaria is caused by Plasmodium species, whose transmission to vertebrate hosts is facilitated by mosquito vectors. The transition from the cold blooded mosquito vector to the host represents physiological stress to the parasite, and additionally malaria blood stage infection is characterised by intense fever periods. In recent years, it has become clear that heat shock proteins play an essential role during the parasite's life cycle. Plasmodium falciparum expresses two prominent heat shock proteins: heat shock protein 70 (PfHsp70) and heat shock protein 90 (PfHsp90). Both of these proteins have been implicated in the development and pathogenesis of malaria. In eukaryotes, Hsp70 and Hsp90 proteins are functionally linked by an essential adaptor protein known as the Hsp70–Hsp90 organising protein (Hop). In this study, recombinant P. falciparum Hop (PfHop) was heterologously produced in E. coli and purified by nickel affinity chromatography. Using specific anti-PfHop antisera, the expression and localisation of PfHop in P. falciparum was investigated. PfHop was shown to co-localise with PfHsp70 and PfHsp90 in parasites at the trophozoite stage. Gel filtration and coimmunoprecipitation experiments suggested that PfHop was present in a complex together with PfHsp70 and PfHsp90. The association of PfHop with both PfHsp70 and PfHsp90 suggests that this protein may mediate the functional interaction between the two chaperones