Executive Summary : | The research aims to understand the transcriptional and posttranslational regulation during growth and development in Dictyostelium discoideum. The study focuses on the regulators of protein function, Peptidyl-prolyl cis/trans isomerases (PPIases), which catalyze isomerisation of Ser/Thr-Pro bonds in peptides and proteins. The four families reported include Cyclophilins, FK506 Binding proteins (FKBPs), Parvulins, and Phosphotyrosyl phosphatase (2A) activator (PTPA). Parvulins, such as human Pin1 and S. cerevisiae Ess1, can recognize phosphorylated Ser/Thr-Pro bonds and have a profound effect on protein stability, activity, subcellular localization, phosphorylation status, protein-protein interactions, and transcriptional activity. Dictyostelium discoideum cells undergo a transition from unicellular to multicellular structures upon nutrient starvation, requiring transcriptional change. The study initiated by the researchers on Parvulin PPIase in D. discoideum found that prolyl isomerisation is important in cellular processes. However, cells with loss of PinA are viable and exhibit a mild phenotype, suggesting that a second parvulin, Pin4, or other PPIases may be compensating its function. The research project aims to investigate the function of Pin4 in D. discoideum using a combination of Molecular and Biochemical techniques, gene deletion, mutation, and overexpression. Interaction studies and activity assays will be performed to identify interacting proteins and cellular pathways, allowing for a better understanding of its role in cellular processes such as cell-cell interaction, cell sorting and patterning, and cell differentiation. |