Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.603734
Title: Evolution of ATP synthase
Author: Harrington, R. A.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 2009
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Abstract:
The hypothesis of modular evolution of the atp operon is re-evaluated by conducting a phylogenetic analysis of the atp operons and constituent genes of all fully sequenced genomes. Although the original hypothesis of modular evolution cannot be conclusively supported, a number of novel observations are made. Foremost is that the atp operon is a mosaic operon, a result of extensive horizontal transfer. In addition, two independent duplication events are proposed for subunits b/b’ of the enzyme, the transmembrane subunits I and z are shown to be more prevalent than previously thought, and an α/β gene pair is proposed as a putative ancestral gene duplication for these catalytic subunits. Further studies investigate the evolution and current importance of the P-loop domain, the nucleotide binding domain found with the α and β subunits of ATP synthase. A database has been developed to annotate the structure-function relationships of protein structural domains on a large-scale basis, including a novel facility to describe these relationships in terms of their taxonomic distribution. It is used in conjunction with the previously created PSIMAP structural interaction database and taxonomy databases to describe the P-loop as consistently one of the most diverse domains in the proteome. It is also represented by nodes at critical positions within both the structural interaction network, and a novel protein structure-function bipartite network, which supports the proposal that it is among the oldest and most successful of all domains. The final chapter presents case studies of three P-loop families, and explains the diversity of function, interaction partners and taxonomic distribution exhibited in terms of their structures and sequences. In particular a novel study comparing and contrasting the pore structures of all P-loop rings is presented, and partially conserved motifs in the G-proteins are described to explain their interactivity.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.603734  DOI: Not available
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