title: Gender and sexuality I: Genderqueer geographies?

authors: Johnston, Lynda

subjects: Social Sciences

abstract: This review considers gender diversity across a range of spaces and places. I note that while the notion of gender has been troubled, there exists opportunities to trouble it further. I highlight the scholarship that has sought to deconstruct genders, and the binary framing of man/woman and male/female roles and relationships. The queering of sexuality has meant that geographers are now tracing the ways in which lesbian, gay, bisexual, transgender, intersex, queer (LGBTIQ) bodies experience and live their gender beyond normative binaries. Research concerned with relational gendered subjectivities within LGBTIQ communities is discussed, and I flag the trend that this research may conflate gendered experiences while privileging sexual subjectivities. Finally, I turn to the recent interest by geographers who - drawing on queer and trans* theories - argue for new and innovative understandings of gender diversity.

text: Gender and sexuality I: Genderqueer geographies? This review considers gender diversity across a range of spaces and places. I note that while the notion of gender has been troubled, there exists opportunities to trouble it further. I highlight the scholarship that has sought to deconstruct genders, and the binary framing of man/woman and male/female roles and relationships. The queering of sexuality has meant that geographers are now tracing the ways in which lesbian, gay, bisexual, transgender, intersex, queer (LGBTIQ) bodies experience and live their gender beyond normative binaries. Research concerned with relational gendered subjectivities within LGBTIQ communities is discussed, and I flag the trend that this research may conflate gendered experiences while privileging sexual subjectivities. Finally, I turn to the recent interest by geographers who - drawing on queer and trans* theories - argue for new and innovative understandings of gender diversity.

year: 2016

title: Mechanism of RNA cleavage by VapC from Pyrobaculum aerophilum

authors: Duyvestyn, Johanna Maria

subjects: VapBC

abstract: Proteins belonging to the PIN-domain family are widespread across bacteria, archaea and eukaryotes. PIN-domain structures are well characterised and contain three highly conserved acidic residues that are orientated to form the active site of the enzyme. VapC is the toxic component of a toxin-antitoxin (TA) complex, and contains a PIN-domain. The VapBC TAs are the largest TA family, and are found in expanded copy numbers in a variety of unrelated organism including the human pathogen Mycobacterium tuberculosis. It is proposed that TAs play a role in metabolic regulation, under conditions of stress. VapCs are metal dependent endoribonucleases that target specific sequences in single stranded RNA and inhibit translation by degrading mRNA transcripts. The mechanism by which VapC cleaves RNA and achieves this specificity is unknown.
 
In this thesis, VapC 2754 from Pyrobaculum aerophilum (VapCPAE2754) is analysed, and a mechanism for catalysis of RNA cleavage by PIN-domains is proposed. Mutations were made to conserved residues in the putative active site to test the hypothesized mechanism. A fluorometric kinetic assay was designed to allow differences in activity to be accurately determined, so that conclusions about the effect of the mutations could be drawn. Mutations made to the conserved acidic amino acids eliminated RNase activity, confirming that these residues are essential to catalysis. A structure for the wild-type VapCPAE2754 was determined, containing cadmium ions and an acetate bound into the active site.

Knowledge of the enzymatic mechanism of PIN domains will enable a greater understanding of this important protein family, and serve as the basis for future drug design by transition state analogue inhibiters. This is especially important in VapC enzymes due to their proposed role in the pathology of M. tuberculosis.

text: Mechanism of RNA cleavage by VapC from Pyrobaculum aerophilum Proteins belonging to the PIN-domain family are widespread across bacteria, archaea and eukaryotes. PIN-domain structures are well characterised and contain three highly conserved acidic residues that are orientated to form the active site of the enzyme. VapC is the toxic component of a toxin-antitoxin (TA) complex, and contains a PIN-domain. The VapBC TAs are the largest TA family, and are found in expanded copy numbers in a variety of unrelated organism including the human pathogen Mycobacterium tuberculosis. It is proposed that TAs play a role in metabolic regulation, under conditions of stress. VapCs are metal dependent endoribonucleases that target specific sequences in single stranded RNA and inhibit translation by degrading mRNA transcripts. The mechanism by which VapC cleaves RNA and achieves this specificity is unknown.
 
In this thesis, VapC 2754 from Pyrobaculum aerophilum (VapCPAE2754) is analysed, and a mechanism for catalysis of RNA cleavage by PIN-domains is proposed. Mutations were made to conserved residues in the putative active site to test the hypothesized mechanism. A fluorometric kinetic assay was designed to allow differences in activity to be accurately determined, so that conclusions about the effect of the mutations could be drawn. Mutations made to the conserved acidic amino acids eliminated RNase activity, confirming that these residues are essential to catalysis. A structure for the wild-type VapCPAE2754 was determined, containing cadmium ions and an acetate bound into the active site.

Knowledge of the enzymatic mechanism of PIN domains will enable a greater understanding of this important protein family, and serve as the basis for future drug design by transition state analogue inhibiters. This is especially important in VapC enzymes due to their proposed role in the pathology of M. tuberculosis.

year: 2012

title: E pā tō reo e Te Matatini, Herewini Parata

authors: Maxwell, Te Kahautu

abstract: Waita ā-ringa (action song) Lyrics composed by Te Kahautu Maxwell, Musical score composed by Te Whānau Mitai, Eric Kurei. Performed by Ōpōtiki Mai Tawhiti (Kapa Haka group) (3mins)

Waiata ā Tira: Aroha
Whakaeke: Pinepine Te Kura, Hau Te Kura
Mōteatea: Te Ao o Te Pārerā
Waiata ā Ringa: E pā to reo, Te Matatini, Herewini Parata
Poi: E ia e ia
Haka: Te Kōtiritiri, Te Kōtaratara
Whakawātea: Ōranga Tōiti, tōnui kōrero

text: E pā tō reo e Te Matatini, Herewini Parata Waita ā-ringa (action song) Lyrics composed by Te Kahautu Maxwell, Musical score composed by Te Whānau Mitai, Eric Kurei. Performed by Ōpōtiki Mai Tawhiti (Kapa Haka group) (3mins)

Waiata ā Tira: Aroha
Whakaeke: Pinepine Te Kura, Hau Te Kura
Mōteatea: Te Ao o Te Pārerā
Waiata ā Ringa: E pā to reo, Te Matatini, Herewini Parata
Poi: E ia e ia
Haka: Te Kōtiritiri, Te Kōtaratara
Whakawātea: Ōranga Tōiti, tōnui kōrero

year: 2023-02-22