The growing problem of antibiotic resistance has prompted the need for new and novel antimicrobial therapies. The bacterial cell division pathway holds great promise for the development of novel broad-spectrum antibiotics as the majority of the proteins are essential for viability. The wealth of information regarding bacterial cell division has come from studies of the model organisms Escherichia coli and Bacillus subtilis. Although much has been elucidated regarding this pathway, the functions of many individual proteins remain unsolved. An important model organism for the investigation of cell division is Streptomyces coelicolor. The mycelial Streptomyces are sporulating, Gram-positive bacteria that grow in long branching networks of filamentous cells much like filamentous fungi. The normally essential process of cell division is dispensable for growth and viability of S. coelicolor. More interestingly, there are two different modes of cell division in this organism, one for vegetative growth and one is utilized for synchronous septation during sporulation. It is still unclear how developmental regulators control this switch, but advancements in fluorescence microscopy have shed some insight into the cell division process by allowing direct visualization of many cellular components and their dynamics. To better understand bacterial cell division and its regulation in S. coelicolor, three additional fluorescent proteins (FPs), including m.RFP, CyPet and YPet, have been established in this work. An m.RFP shuttle vector was constructed and the utility of m.RFP was tested by translationally fusing it to a tip-localizing protein, DiviVA. This work demonstrated that m.RFP is functional and an efficient marker for localized proteins. Also, established in this work is a two-colour fluorescence reporter system, which includes the fluorescent proteins CyPet and YPet that can be used to study co-localization and protein-protein interactions within cells. Future plans are to use co-localization of FP fusions and fluorescence resonance energy transfer (FRET) between CyPet and YPet to investigate the assembly of protein complexes within the cells, such as those involved in cell division. These studies will reveal critical information that is needed for the development of drugs that have novel mechanisms of action. / Thesis / Master of Science (MSc)