128 research outputs found

    Integrating Art and Science in Undergraduate Education

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    The prevailing vision for undergraduate science education includes increased collaboration among teachers of science, technology, engineering and math (STEM) and an overhaul of introductory courses [1]–[4]. But by staying within the borders of STEM, are we overlooking connections between the arts and innovative science? Likewise, are we missing an important opportunity to inspire and inform nonscientists? Here we explore how weaving the visual arts into a science curriculum can both help develop scientific imagination and engage nonscientists. As an example, we describe a recent collaboration between artists and scientists to create a series of science-inspired sculptures

    Automatic Animation of Molecular Motion using Python and Cinema 4D

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    Expression of Lactate Dehydrogenase (LDHA) WT and A320T Mutant

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    The human genome has a length of approximately 3 billion base pairs, containing a total of over 20,000 genes, which can all be subjected to mutations that cause variations in the genome. Variations in a genome can be potentially either benign or pathogenic, but it can be difficult to distinguish whether a variant is one or the other, leading to tens of thousands being classified as variants of unknown significance (VUS). Our lab was particularly interested in the VUSs in lactate dehydrogenase (LDHA), an oxidoreductase enzyme that catalyzes the reversible conversion of pyruvate to lactate, an important component to anaerobic metabolism. Our lab is focusing on the A320T (alanine to threonine mutation at position 320) VUS, in which we cultured BL21 (DE3) and DH5α E. coli cell strains, so that we are able to clone wild type (WT) and A320T mutant enzymes. We eventually expressed and purified the two types of LDHA to observe the activity of each. Through expression and purification of both wild type and mutated forms of LDHA, we can observe the impact that the A320T-mutated VUS will have on the function of the LDHA protein, thus determining whether the VUS is benign or pathogenic to the enzyme function

    Informal Trading Infrastructure and Management

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    Our goal was to make recommendations for infrastructure designs and management options for informal traders to be used in the central business district (CBD) of Mitchells Plain in Cape Town, South Africa. We interviewed traders in the marketplace to communicate their concerns and suggestions to the City. We proposed canopy options and management improvements for the market. This project produced proposals for improvement in four main areas; infrastructure, waste management, merchandise transportation and storage. With implementation, the recommendations would improve the functionality of the marketplace

    Effective Radial Thermal Conductivity in Fixed-Bed Reactor Tubes

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    The purpose of our research is to more accurately model the temperature gradient across a fixed bed reactor used in steam-methane reforming. Heat transfer in the near-wall region was modeled using computational fluid dynamics. Heat transfer in the bed center region was determined through analysis of measured temperature profiles in a packed bed. Using this two-region approach, the effective radial thermal conductivity was used in a 2D pseudo-homogeneous heat-transfer model solved by finite element method and compared to experimental temperatures

    \u3ci\u3eParamecium bursaria\u3c/i\u3e Chlorella Virus 1 Encodes a Polyamine Acetyltransferase

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    Background: PBCV-1 gene a654l encodes a protein with sequence similarity to GCN5 histone acetyltransferases. Results: A crystal structure of A654L bound to coenzyme A reveals how A654L acetylates polyamines, not histone lysines. Conclusion: A654L functions as a polyamine acetyltransferase. Significance: As the first viral polyamine acetyltransferase, A654L has a possible role in host polyamine catabolism in viral replication. Paramecium bursaria chlorella virus 1 (PBCV-1), a large DNA virus that infects green algae, encodes a histone H3 lysine 27-specific methyltransferase that functions in global transcriptional silencing of the host. PBCV-1 has another gene a654l that encodes a protein with sequence similarity to the GCN5 family histone acetyltransferases. In this study, we report a 1.5AËš crystal structure of PBCV-1 A654L in a complex with coenzyme A. The structure reveals a unique feature of A654L that precludes its acetylation of histone peptide substrates. We demonstrate that A654L, hence named viral polyamine acetyltransferase (vPAT), acetylates polyamines such as putrescine, spermidine, cadaverine, and homospermidine present in both PBCV-1 and its host through a reaction dependent upon a conserved glutamate 27. Our study suggests that as the first virally encoded polyamine acetyltransferase, vPAT plays a possible key role in the regulation of polyamine catabolism in the host during viral replication. Includes Supplemental Material

    \u3ci\u3eParamecium bursaria\u3c/i\u3e Chlorella Virus 1 Encodes a Polyamine Acetyltransferase

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    Background: PBCV-1 gene a654l encodes a protein with sequence similarity to GCN5 histone acetyltransferases. Results: A crystal structure of A654L bound to coenzyme A reveals how A654L acetylates polyamines, not histone lysines. Conclusion: A654L functions as a polyamine acetyltransferase. Significance: As the first viral polyamine acetyltransferase, A654L has a possible role in host polyamine catabolism in viral replication. Paramecium bursaria chlorella virus 1 (PBCV-1), a large DNA virus that infects green algae, encodes a histone H3 lysine 27-specific methyltransferase that functions in global transcriptional silencing of the host. PBCV-1 has another gene a654l that encodes a protein with sequence similarity to the GCN5 family histone acetyltransferases. In this study, we report a 1.5AËš crystal structure of PBCV-1 A654L in a complex with coenzyme A. The structure reveals a unique feature of A654L that precludes its acetylation of histone peptide substrates. We demonstrate that A654L, hence named viral polyamine acetyltransferase (vPAT), acetylates polyamines such as putrescine, spermidine, cadaverine, and homospermidine present in both PBCV-1 and its host through a reaction dependent upon a conserved glutamate 27. Our study suggests that as the first virally encoded polyamine acetyltransferase, vPAT plays a possible key role in the regulation of polyamine catabolism in the host during viral replication. Includes Supplemental Material

    Virus–host interactions: insights from the replication cycle of the large \u3ci\u3eParamecium bursaria\u3c/i\u3e chlorella virus

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    The increasing interest in cytoplasmic factories generated by eukaryotic-infecting viruses stems from the realization that these highly ordered assemblies may contribute fundamental novel insights to the functional significance of order in cellular biology. Here, we report the formation process and structural features of the cytoplasmic factories of the large dsDNA virus Paramecium bursaria chlorella virus 1 (PBCV-1). By combining diverse imaging techniques, including scanning transmission electron microscopy tomography and focused ion beam technologies, we show that the architecture and mode of formation of PBCV-1 factories are significantly different from those generated by their evolutionary relatives Vaccinia and Mimivirus. Specifically, PBCV-1 factories consist of a network of single membrane bilayers acting as capsid templates in the central region, and viral genomes spread throughout the host cytoplasm but excluded from the membranecontaining sites. In sharp contrast, factories generated by Mimivirus have viral genomes in their core, with membrane biogenesis region located at their periphery. Yet, all viral factories appear to share structural features that are essential for their function. In addition, our studies support the notion that PBCV-1 infection, which was recently reported to result in significant pathological outcomes in humans andmice, proceeds througha bacteriophage -like infection pathway

    Chlorella Virus PBCV-1 Encodes a Functional Homospermidine Synthase

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    Sequence analysis of the 330-kb genome of chlorella virus Paramecium bursaria chlorella virus 1 (PBCV-1) revealed an open reading frame, A237R, that encodes a protein with 34% amino acid identity to homospermidine synthase from Rhodopseudomonas viridis. Expression of the a237r gene product in Escherichia coli established that the recombinant enzyme catalyzes the NAD+-dependent formation of homospermidine from two molecules of putrescine. The a237r gene is expressed late in PBCV-1 infection. Both uninfected and PBCV-1-infected chlorella, as well as PBCV-1 virions, contain homospermidine, along with the more common polyamines putrescine, spermidine, and cadaverine. The total number of polyamine molecules per virion (~539) is too small to significantly neutralize the virus double-stranded DNA (\u3e660,000 nucleotides). Consequently, the biological significance of the homospermidine synthase gene is unknown. However, the gene is widespread among the chlorella viruses. To our knowledge, this is the first report of a virus encoding an enzyme involved in polyamine biosynthesis

    Identification of an L-Rhamnose Synthetic Pathway in Two Nucleocytoplasmic Large DNA Viruses

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    Nucleocytoplasmic large DNA viruses (NCLDVs) are characterized by large genomes that often encode proteins not commonly found in viruses. Two species in this group are Acanthocystis turfacea chlorella virus 1 (ATCV-1) (family Phycodnaviridae, genus Chlorovirus) and Acanthamoeba polyphaga mimivirus (family Mimiviridae), commonly known as mimivirus. ATCV-1 and other chlorovirus members encode enzymes involved in the synthesis and glycosylation of their structural proteins. In this study, we identified and characterized three enzymes responsible for the synthesis of the sugar L-rhamnose: two UDP-D-glucose 4,6-dehydratases (UGDs) encoded by ATCV-1 and mimivirus and a bifunctional UDP-4-keto-6-deoxy-D-glucose epimerase/reductase (UGER) from mimivirus. Phylogenetic analysis indicated that ATCV-1 probably acquired its UGD gene via a recent horizontal gene transfer (HGT) from a green algal host, while an earlier HGT event involving the complete pathway (UGD and UGER) probably occurred between a protozoan ancestor and mimivirus. While ATCV-1 lacks an epimerase/reductase gene, its Chlorella host may encode this enzyme. Both UGDs and UGER are expressed as late genes, which is consistent with their role in posttranslational modification of capsid proteins. The data in this study provide additional support for the hypothesis that chloroviruses, and maybe mimivirus, encode most, if not all, of the glycosylation machinery involved in the synthesis of specific glycan structures essential for virus replication and infection
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