Did the organellar transit peptide duplicate itself to make a disordered linker protein?
We propose to verify if LCI5, a protein that plays a pivotal role in carbon concentration mechanism (CCM), evolved by duplication of transit peptide encoding sequences. We hypothesize that the intrinsically disordered nature of transit peptides could make them ideal motifs for inter-protein interactions. Therefore, we also propose to check if transit-peptide like sequences occur in the non-N- terminal regions of proteins. Our studies will not only give new insights about evolution of transit peptides, they will also help protein engineers with design of scaffolding proteins and interactors.