title: Coverpage and Contents

authors: Waikato Geological Society

abstract: Coverpage and Contents from Volume 4, Number 1, 1970 of Earth Science Journal.

text: Coverpage and Contents Coverpage and Contents from Volume 4, Number 1, 1970 of Earth Science Journal.

year: 1970

title: The DNA Binding Protein Lsr2 from Mycobacterium tuberculosis

authors: Summers, Emma Louise

subjects: DNA binding protein

abstract: Lsr2 is a small, basic DNA binding protein that is highly conserved in mycobacteria and related actinomycetes. Lsr2 is essential for growth in Mycobacterium tuberculosis and previous studies have shown that Lsr2 is involved in down-regulating a wide range of genes involved in cell wall synthesis and metabolic functions. This regulatory function is likely to influence bacterial growth and survival.

This research investigated the biochemistry and 3D structure of Lsr2 from M. tuberculosis. Transmission electron microscopy (TEM) analysis of Lsr2 in complex with DNA revealed a regular fibril-like arrangement of protein coating double-stranded DNA. In addition, it was shown that Lsr2 physically protected DNA from DNase activity. The structure of the C-terminal DNA binding domain of Lsr2, determined by others part way through this research, prompted site directed mutagenesis of residues proposed to interact with DNA. Modification of arginine residues significantly reduced the binding of Lsr2 to DNA and fibril-like structures were not observed using TEM, for arginine mutants.

The first crystal structure of the N-terminal domain of Lsr2 is reported here. Two high resolution structures in monoclinic and hexagonal space groups were solved using X-ray crystallography and ab initio phasing. Proteolytic processing of the N-terminus of Lsr2 was revealed by the structure in P2₁ and this process was recreated using the protease trypsin which resulted in crystal formation in a P3₁21 space group. Both structures show linear chains of dimeric N-terminal Lsr2, as shown by crystallographic symmetry, linked by overlapping anti-parallel β-sheets, revealing a mechanism of protein oligomerisation. Oligomerisation only occurs after the removal of the first three residues M1, A2 and K3. In solution, protein oligomerisation was recreated with trypsin, resulting in the formation of large protein complexes. A change in DNA topology after the addition of trypsin to full-length Lsr2/DNA complexes was observed using TEM. This mechanism is likely to be important to M. tuberculosis under “stress” conditions where proteases are known to be upregulated and where cross-linking and condensation of DNA is critical.

text: The DNA Binding Protein Lsr2 from Mycobacterium tuberculosis Lsr2 is a small, basic DNA binding protein that is highly conserved in mycobacteria and related actinomycetes. Lsr2 is essential for growth in Mycobacterium tuberculosis and previous studies have shown that Lsr2 is involved in down-regulating a wide range of genes involved in cell wall synthesis and metabolic functions. This regulatory function is likely to influence bacterial growth and survival.

This research investigated the biochemistry and 3D structure of Lsr2 from M. tuberculosis. Transmission electron microscopy (TEM) analysis of Lsr2 in complex with DNA revealed a regular fibril-like arrangement of protein coating double-stranded DNA. In addition, it was shown that Lsr2 physically protected DNA from DNase activity. The structure of the C-terminal DNA binding domain of Lsr2, determined by others part way through this research, prompted site directed mutagenesis of residues proposed to interact with DNA. Modification of arginine residues significantly reduced the binding of Lsr2 to DNA and fibril-like structures were not observed using TEM, for arginine mutants.

The first crystal structure of the N-terminal domain of Lsr2 is reported here. Two high resolution structures in monoclinic and hexagonal space groups were solved using X-ray crystallography and ab initio phasing. Proteolytic processing of the N-terminus of Lsr2 was revealed by the structure in P2₁ and this process was recreated using the protease trypsin which resulted in crystal formation in a P3₁21 space group. Both structures show linear chains of dimeric N-terminal Lsr2, as shown by crystallographic symmetry, linked by overlapping anti-parallel β-sheets, revealing a mechanism of protein oligomerisation. Oligomerisation only occurs after the removal of the first three residues M1, A2 and K3. In solution, protein oligomerisation was recreated with trypsin, resulting in the formation of large protein complexes. A change in DNA topology after the addition of trypsin to full-length Lsr2/DNA complexes was observed using TEM. This mechanism is likely to be important to M. tuberculosis under “stress” conditions where proteases are known to be upregulated and where cross-linking and condensation of DNA is critical.

year: 2012

title: Māori women’s perspectives of leadership and wellbeing

authors: Ruru, Stacey Mariu

subjects: Māori leadership

abstract: Within Aotearoa, New Zealand, Māori women are engaged in leadership roles in community and professional workplace settings, however little is known about how they maintain their wellbeing. This research sought to unravel how Māori women leaders maintain their wellbeing, while occupied in complex leadership roles. We report on the findings from semi-structured interviews, acknowledging kaupapa Māori theory and principles, with five Māori women leaders. Thematic analysis was used, and these themes related to five whakataukī (proverb) that provided overarching themes and directions relating to Māori women’s leadership and wellbeing. Each whakataukī describe unique aspects of leadership and wellbeing from a Māori worldview. Themes include humility, collectiveness, courage, future orientations and positivity. While the themes are housed in whakataukī, central to the success of these Māori women leaders was being connected to whānau (family) and friends, and being influenced by tamariki (children), tauira (students) and employees. These social connections made Māori women leaders strong and resilient to change and challenges.

text: Māori women’s perspectives of leadership and wellbeing Within Aotearoa, New Zealand, Māori women are engaged in leadership roles in community and professional workplace settings, however little is known about how they maintain their wellbeing. This research sought to unravel how Māori women leaders maintain their wellbeing, while occupied in complex leadership roles. We report on the findings from semi-structured interviews, acknowledging kaupapa Māori theory and principles, with five Māori women leaders. Thematic analysis was used, and these themes related to five whakataukī (proverb) that provided overarching themes and directions relating to Māori women’s leadership and wellbeing. Each whakataukī describe unique aspects of leadership and wellbeing from a Māori worldview. Themes include humility, collectiveness, courage, future orientations and positivity. While the themes are housed in whakataukī, central to the success of these Māori women leaders was being connected to whānau (family) and friends, and being influenced by tamariki (children), tauira (students) and employees. These social connections made Māori women leaders strong and resilient to change and challenges.

year: 2017