Emir Maldosevic, a graduate student in the Jomaa lab, has won the Michael J. Peach Award for 2026. This annual award is made to a graduate student who embodies enthusiasm for research and the principles of sharing and collaboration.
Emir earned his BS in Biology and Chemistry with honors from the University of North Florida. He joined the lab of Dr. Ahmad Jomaa, Assistant Professor, Molecular Physiology and Biological Physics, in February 2023. The lab investigates fundamental co-translational mechanisms that regulate protein synthesis, protein targeting, and protein homeostasis, processes that are central to cellular physiology and human health.
We asked Emir to tell us about his research and his hopes for the future. Here’s what he said.
Can you tell us about your research?
My research focuses on understanding how cells regulate translation and ensure that newly made proteins reach the correct cellular compartments as they are being synthesized. In the Jomaa lab, I use structural and biochemical approaches to directly visualize how the ribosome interacts with the regulatory elements, factors, and chaperones that guide these processes.
Ribosomes do more than translate mRNA into protein, they can sense regulatory features in mRNAs or emerging nascent chains to control protein production. Our recent work shows how a conserved sequence in the mRNA encoding AMD1, a key enzyme in polyamine biosynthesis, regulates its own production through programmed ribosome stalling. Structural analysis revealed that a short segment of the C-terminal tail acts as a molecular brake inside the ribosome, temporarily pausing translation. Understanding how AMD1 synthesis is controlled during translation may reveal new ways to control AMD1 expression and polyamine metabolism in cancers where these pathways are dysregulated.
My work also examines how newly made proteins are directed to the correct location in the cell. Many proteins must be accurately delivered to specific compartments, such as mitochondria, and errors in this process can impair mitochondrial function. As nascent proteins emerge from the ribosome, they encounter factors and chaperones that guide their folding, processing, and localization. We recently showed that the nascent polypeptide-associated complex, or NAC, acts as a molecular gatekeeper that helps prevent mitochondrial proteins from being incorrectly delivered to the endoplasmic reticulum. Together, these studies highlight how the ribosome serves as an active decision-making hub that helps cells regulate both protein synthesis and protein localization.
What drives or motivates your scientific pursuits?
When I started graduate school, I was captivated by the idea of seeing biology happen at the molecular level. Learning cryo-electron microscopy in the Jomaa lab gave me a way to look directly at the molecular machines that build the proteins our cells rely on. Connecting these molecular snapshots to broader physiological questions, including how these processes become disrupted in disease, has been one of the most rewarding parts of my graduate training. I am grateful for the mentorship and collaborative community at UVA, which have helped me grow as a scientist and prepare for the next stage of my career.
What are your future goals?
Looking ahead, I am excited to continue applying structural approaches to understand how these pathways support normal cell function and how they become disrupted in disease. As technology advances, we are also moving closer to visualizing these processes directly inside cells, which will help fill important gaps in our understanding of the biological mechanisms that maintain human health.
Congratulations on winning this award, Emir!