According to Kaji and his colleagues, RRF binds to different locations within the ribosomal complex at different times. It seems that, if the ribosome is the protein factory, the RRF is the foreman, moving from location to location to 'supervise' the end of the assembly line. When the new protein is completed, RRF works in conjunction with other proteins to disassemble the ribosomal complex so that the components of the machinery are ready for the next round of protein creation.
Kaji believes that, since RRF plays the key role only in bacteria and mitochondria, the bacterial protein also provides an interesting target for new types of anti-bacterial agents. His research has already shown in the laboratory that bacteria lacking RRF cannot exist because of their inability to create new proteins.
"As bacteria mutate to become resistant to antibiotics, we must keep targeting parts of bacteria that are integral for functioning so that bacteria can not out-evolve antibiotics," said Kaji. "We are considering RRF as the target of a new type of antibiotic, an inhibitor of RRF that we can easily alter as bacteria become resistant."