Defined spatial distribution of proteins plays a major role in nature, like structures for bacterial cell mobility (Escherichia coli’s flagella), capsid structures of viruses, structures for the controlled segregation of chromosomal DNA both in eukaryotic and prokaryotic cells, a large array of membrane protein complexes (e.g. protein transporters and nutrient transporters) and the assembly of channeled metabolic pathways among many others. All these diverse and fundamental processes are the result of the evolution of very specific and controlled spatial organization of multiple proteins. Defined spatial distribution also plays a major role in many biotechnological applications of proteins, from the immobilization of antibodies on the surface of an electrode for their use in biosensors to the creation of nanostructures through biotemplating. A wide variety of approaches have been developed in order to allow the easy immobilization of proteins, ranging from electrostatic interactions and direct covalent linkage to high affinity non-covalent interactions (e.g. streptavidin/biotin). In order to facilitate the generation of more complex synthetic quaternary protein structures (on surfaces and in solution), we propose the development of a protein fusion tag system that will enable the controlled and orderly precise co-immobilization of proteins by means of protein-DNA interactions. This project aims to take advantage of the highly developed methodologies that currently exist and allow the synthesis and immobilization of DNA with ease and use them as a means for controlled protein co-immobilization. Specifically, to achieve this objective, we propose to develop a panel of high affinity DNA binding proteins with different sequence specificities to be used as fusion tags and provide the protein-DNA interaction link.