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Hasan Koc Laboratory

Proteomics of mitochondrial translation

Mitochondrial translation plays a key role in energy production due to its crucial role in synthesizing 13 proteins employed in oxidative phosphorylation.  These proteins form the hydrophobic core of Complexes I, III, IV, V (ATP Synthase) in the inner membrane of mitochondria.   The 55S mitochondrial ribosomes, which are close relatives of their bacterial counterparts, consist of small 28S and large 39S subunits.  Over 90% of a eukaryotic cell’s energy is produced from oxidative phosphorylation.  This fact puts the mitochondrial ribosomes in charge of the energy metabolism and gives a critical regulatory role.   Our central hypothesis is that alterations in the function of mitochondrial ribosomes will have a consequence on energy production.   In fact, the studies from our laboratory and others have demonstrated links between structural changes in the mitochondrial ribosomes and oxidative phosphorylation.  These changes have either been in the form of a change in the protein composition of the ribosome or a post-translational modification.  Our recent work has focused on investigating these changes in the proteins of mitochondrial ribosomes and associated proteins and determining their effects on the changes or the remodeling of mitochondrial energy metabolism.   Furthermore, we have shown correlations between alterations in mitochondrial energy metabolism in disease including various forms of cancer.