Undergraduate Honors Thesis


Biochemical Characterization of the Human Transmembrane 70 Protein Public Deposited

  • Mitochondria are dynamic cellular organelles involved in energy production, cell signaling, and regulated cell death. Mitochondria are double-membrane-bound organelles, consisting of both inner and outer membranes. Invaginations of the mitochondrial inner membrane, called cristae, are major sites of energy production due to the large number of adenosine triphosphate (ATP) synthases, which create ATP, an organic compound that fuels chemical processes in the body. Previous studies have shown that transmembrane protein 70 (TMEM70) is involved in stabilizing the formation of the c8-ring of ATP synthase, which is critical for ATP production through Oxidative Phosphorylation (OXPHOS) in mitochondria. TMEM70 deficiency causes mitochondrial encephalo-cardiomyopathy, a disease that can cause cardiac arrhythmias and cardiac failure, shorter lifespans, and other debilitating symptoms. However, the precise role of TMEM70 in mitochondria, as well as the molecular mechanisms that regulate the biogenesis of ATP synthase, remain incompletely understood. To begin to understand the role of TMEM70 in the biogenesis of ATP synthase, we characterized the biochemical and structural properties of human TMEM70 through protein purification and negative-stain electron microscopy (EM). This study specifically provides the basis for future studies into the 3D structure of TMEM70 and more broadly offers a model for the purification of transmembrane proteins. Understanding the structure of this protein offers insight into the biological mechanism of TMEM70 and may provide a novel point of intervention to offset TMEM70 deficiency and its symptoms. 

Date Awarded
  • 2022-04-05
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Granting Institution
Last Modified
  • 2022-04-12
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