Project description

The bacterial cytoplasm has a crowded and dynamic environment in which the organization of proteins can influence molecular diffusion and biochemical reactions. Recent research has shown that proteins involved in amino acid metabolism, particularly those belonging to the Clusters of Orthologous Groups (COG) category E, can form amorphous protein agglomerates. (Condition-dependent amorphous protein agglomerates control cytoplasmic rheology Molecular Cell, 2026) These agglomerates have been associated with changes in cytoplasmic diffusion and viscoelasticity, as COG-E proteins are involved in synthesis of amino acids which are the building block of the cell, which raises important questions as to why and how they are forming. To answer them we aim to investigate the mechanisms governing the formation and dissolution of protein agglomerates, their effects on enzyme catalytic activity, and their impact on metabolic flux. Ultimately, this research aims to understand how enzyme organization influences cytoplasmic viscoelasticity and metabolic regulation.