Author                                                                                                                              
 

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Reshmi Sinha

Anthropology and
Biological Sciences

During the summer after her freshman year, Reshmi discovered the opportunity for research that led her to work at UCI’s Cumsky Laboratory. According to Reshmi, participating in research has enhanced her education in more than a few ways, and has given her a foundation for pursuing her goal of attending medical school. “I have been made aware of the limitless scope of research and the potential impact it can have on everyday life,” she says. She is an active member of UCI’s Flying Samaritans, enjoys playing the piano and collecting first edition books. triangle.gif (504 bytes)

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Abstract                                                                                                                           
 

The biogenesis of functional mitochondria is essential to the survival of all eukaryotic cells. Mitochondria are organelles whose chief function is to supply a cell with energy in the form of adenosine triphosphate (ATP). The final step in ATP production requires cytochrome c oxidase, a multi-subunit enzyme complex. One of the essential subunits of cytochrome c oxidase is Va. Ongoing studies seek to identify the mitochondrial proteins responsible for the import and sorting of subunit Va to the mitochondrial inner membrane. Past research in the Cumsky laboratory has identified a previously uncharacterized gene named MIA1. This gene is encoded by nuclear DNA, encodes a 16.2 kDa gene product localized in the mitochondrial inner membrane, and is essential for the viability of yeast cells. The goal of this project was to investigate the role of the Mia1 protein (Mia1p) in mitochondrial biogenesis. It was found that cells depleted of Mia1p show loss of respiratory complexes, lose mitochondrial DNA, and display altered mitochondrial morphologies. MIA1 has a human homolog whose product, CG1-136 protein, has 65% similarity in amino acid sequence. Therefore, it is probable that defects in the MIA1 homolog in humans will result in severe disease. Further understanding of protein import and localization in mitochondria may help with the development of therapies that will address such problems.triangle.gif (504 bytes)

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Faculty Mentor                                                                                                                
 
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Michael Cumsky

School of Biological
Sciences

When Reshmi began work on the MIA1 gene, our lab group knew little about it. Her work, and that of her primary collaborator Dr. Virginia Bilanchone, established that MIA1 encodes a protein critical for mitochondrial biogenesis. Furthermore, this work determined the scope and direction of subsequent studies that have confirmed Reshmi’s findings. These studies have shown that the MIA1 protein interacts with proteins of the mitochondrial import motor, and therefore may be a component of this molecular machine. In addition, it was found that a Drosophila homolog of MIA1 causes early embryogenic death in fruit flies when defective. Reshmi’s project is a wonderful example of excellence in undergraduate research. It also underscores the value of this experience for both student and laboratory. Reshmi’s work is a significant contribution to both our laboratory’s research and mitochondrial research in general.triangle.gif (504 bytes)

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