Systematic analysis of prenylation of bacterial proteins by eukaryotic host cells through combination of computational protein sequence analysis with wet-lab experimental verifications.

• Main Author: Chan, Siang Yin.
• Other Authors: School of Biological Sciences
• Format: Final Year Project
• Language: English
• Published: 2011
• Subjects: DRNTU::Science::Biological sciences::Microbiology::Bacteria
• Online Access: http://hdl.handle.net/10356/44505
• Institution: Nanyang Technological University

A C-terminal motif on proteins allows for recognition by at least one of three prenyltransferases for addition of an isoprenyl anchor. This post-translational lipid modification, known as prenylation, facilitates membrane localization and protein-protein interaction. The prenylation enzymes are only found in Eukaryotes but recent findings suggest that there could be some examples of bacterial and viral prenylation through the eukaryotic host. In this project, all available bacterial and viral proteins downloaded from the National Center for Biotechnology (NCBI) protein database with the motif were predicted for the possibility of prenylation with the Prenylation Prediction Suite (PrePS). Subsequently, the most common domains were studied for the possible function of the lipid modification in the protein. Bacterial proteins containing highly conserved eukaryotic domains like DnaJ and SNARE mimic their host cell counterparts, thus interfering their normal function and conferring advantage to the bacteria. Interaction of host cell proteins with an F-box protein already proven to be prenylated was also studied to further understand its function. Prenylation inhibition of bacterial and viral proteins whereby the lipid anchor is important for their survival and replication in the host cell, may become a novel way of inhibiting further infection and disease by these pathogens.