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Phillip Nagley’s more recent work on the formation, structure and function of ATP synthase is carried out in collaboration with Rod Devenish at Monash. In 1988, using subunit 8, this group achieved the first successful functional relocation of a mitochondrial gene to the nucleus. This enabled systematic manipulation in vivo of mitochondrially encoded proteins by site-directed mutagenesis, which had hitherto eluded mitochondrial researchers. Further work by Nagley and colleagues on yeast ATP synthase defined functional aspects, as well as topology and proximity relationships, of subunit 8 and several other proteins, particularly those of the stator stalk of this enzyme complex. Recently, the fluorescence properties of proteins tagged with GFP and its variants have been exploited (particularly by Mark Prescott in the Monash mitochondria research group) to study in novel ways the association of protein subunits within ATP synthase and between different mitochondrial enzyme complexes.
Phillip’s interests extended to the molecular biology of ageing; his work involved the characterisation and quantification of age-associated mtDNA mutations in several human and rat tissues. This research recently led to the recognition of links between accumulation of mtDNA mutations and the age-associated decline in physiological function of tissues (in conjunction with the physiologically and clinically oriented research of Zeinab Khalil and Frank Rosenfeldt).
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Julie D. Atkin,Manal A. Farg,Bradley J. Turner,Doris Tomas, Judith A. Lysaght, Janelle Nunan,Alan Rembach,Phillip Nagley,Philip M. Beart,Surindar S. Cheema,Malcolm K. Horne
JOURNAL OF BIOLOGICAL CHEMISTRYno. 28 (2017)
Journal of neurochemistryno. 1 (2013): 190-204
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