title: A map of the nanoworld: Sizing up the science, politics and business of the infinitesimal

authors: Munshi, Debashish

subjects: nanotechnology

abstract: Mapping out the eight main nodes of nanotechnology discourse that have emerged in the past decade, we explore how various scientific, social, and ethical islands of discussion have developed, been recognized, and are being continually renegotiated. We do so by (1) identifying the ways in which scientists, policy makers, entrepreneurs, educators, and environmental groups draw boundaries on issues relating to nanotechnology; (2) describing concisely the perspectives from which these boundaries are drawn; and (3) exploring how boundaries on nanotechnology are marked and negotiated through contestations of power among various nodes of nanotechnology discourse.

text: A map of the nanoworld: Sizing up the science, politics and business of the infinitesimal Mapping out the eight main nodes of nanotechnology discourse that have emerged in the past decade, we explore how various scientific, social, and ethical islands of discussion have developed, been recognized, and are being continually renegotiated. We do so by (1) identifying the ways in which scientists, policy makers, entrepreneurs, educators, and environmental groups draw boundaries on issues relating to nanotechnology; (2) describing concisely the perspectives from which these boundaries are drawn; and (3) exploring how boundaries on nanotechnology are marked and negotiated through contestations of power among various nodes of nanotechnology discourse.

year: 2007

title: The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection

authors: Summers, Emma Louise

subjects: biology

abstract: Lsr2 is a small DNA-binding protein present in mycobacteria and related actinobacteria that regulates gene expression and influences the organization of bacterial chromatin. Lsr2 is a dimer that binds to AT-rich regions of chromosomal DNA and physically protects DNA from damage by reactive oxygen intermediates (ROI). A recent structure of the C-terminal DNA-binding domain of Lsr2 provides a rationale for its interaction with the minor groove of DNA, its preference for AT-rich tracts, and its similarity to other bacterial nucleoid-associated DNA-binding domains. In contrast, the details of Lsr2 dimerization (and oligomerization) via its N-terminal domain, and the mechanism of Lsr2-mediated chromosomal cross-linking and protection is unknown. We have solved the structure of the N-terminal domain of Lsr2 (N-Lsr2) at 1.73 Å resolution using crystallographic ab initio approaches. The structure shows an intimate dimer of two ß-ß-a motifs with no close homologues in the structural databases. The organization of individual N-Lsr2 dimers in the crystal also reveals a mechanism for oligomerization. Proteolytic removal of three N-terminal residues from Lsr2 results in the formation of an anti-parallel β-sheet between neighboring molecules and the formation of linear chains of N-Lsr2. Oligomerization can be artificially induced using low concentrations of trypsin and the arrangement of N-Lsr2 into long chains is observed in both monoclinic and hexagonal crystallographic space groups. In solution, oligomerization of N-Lsr2 is also observed following treatment with trypsin. A change in chromosomal topology after the addition of trypsin to full-length Lsr2-DNA complexes and protection of DNA towards DNAse digestion can be observed using electron microscopy and electrophoresis. These results suggest a mechanism for oligomerization of Lsr2 via protease-activation leading to chromosome compaction and protection, and concomitant down-regulation of large numbers of genes. This mechanism is likely to be relevant under conditions of stress where cellular proteases are known to be upregulated.

text: The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection Lsr2 is a small DNA-binding protein present in mycobacteria and related actinobacteria that regulates gene expression and influences the organization of bacterial chromatin. Lsr2 is a dimer that binds to AT-rich regions of chromosomal DNA and physically protects DNA from damage by reactive oxygen intermediates (ROI). A recent structure of the C-terminal DNA-binding domain of Lsr2 provides a rationale for its interaction with the minor groove of DNA, its preference for AT-rich tracts, and its similarity to other bacterial nucleoid-associated DNA-binding domains. In contrast, the details of Lsr2 dimerization (and oligomerization) via its N-terminal domain, and the mechanism of Lsr2-mediated chromosomal cross-linking and protection is unknown. We have solved the structure of the N-terminal domain of Lsr2 (N-Lsr2) at 1.73 Å resolution using crystallographic ab initio approaches. The structure shows an intimate dimer of two ß-ß-a motifs with no close homologues in the structural databases. The organization of individual N-Lsr2 dimers in the crystal also reveals a mechanism for oligomerization. Proteolytic removal of three N-terminal residues from Lsr2 results in the formation of an anti-parallel β-sheet between neighboring molecules and the formation of linear chains of N-Lsr2. Oligomerization can be artificially induced using low concentrations of trypsin and the arrangement of N-Lsr2 into long chains is observed in both monoclinic and hexagonal crystallographic space groups. In solution, oligomerization of N-Lsr2 is also observed following treatment with trypsin. A change in chromosomal topology after the addition of trypsin to full-length Lsr2-DNA complexes and protection of DNA towards DNAse digestion can be observed using electron microscopy and electrophoresis. These results suggest a mechanism for oligomerization of Lsr2 via protease-activation leading to chromosome compaction and protection, and concomitant down-regulation of large numbers of genes. This mechanism is likely to be relevant under conditions of stress where cellular proteases are known to be upregulated.

year: 2012

title: An evaluation of Te Rau Puawai workforce 100: Evaluation overview

authors: Nikora, Linda Waimarie

subjects: Maori students

abstract: In July 2001, the Maori & Psychology Research Unit of the University of Waikato was asked to conduct an evaluation of the Te Rau Puawai programme, a joint venture between the former Health Funding Authority and Massey University. The overall goal of the programme is to contribute at least 100 Maori graduates to the Maori mental health workforce within a five year period. The overall aim of the evaluation was to provide the Ministry of Health with a clearer understanding of the programme including: the perceived critical success factors, the barriers if any regarding Te Rau Puawai, the impact of the programme, the extent to which the programme may be transferable, gaps in the programme, and suggested improvements. Through archival search, questionnaire surveys and interviews, evaluative data was collected from major stakeholders in the Te Rau Puawai programme.

text: An evaluation of Te Rau Puawai workforce 100: Evaluation overview In July 2001, the Maori & Psychology Research Unit of the University of Waikato was asked to conduct an evaluation of the Te Rau Puawai programme, a joint venture between the former Health Funding Authority and Massey University. The overall goal of the programme is to contribute at least 100 Maori graduates to the Maori mental health workforce within a five year period. The overall aim of the evaluation was to provide the Ministry of Health with a clearer understanding of the programme including: the perceived critical success factors, the barriers if any regarding Te Rau Puawai, the impact of the programme, the extent to which the programme may be transferable, gaps in the programme, and suggested improvements. Through archival search, questionnaire surveys and interviews, evaluative data was collected from major stakeholders in the Te Rau Puawai programme.

year: 2002-05-01