Termination is beginning to resemble a typical translation mechanism with parallels to other phases of protein synthesis. Concepts such as structural mimicry between the complexes formed at each stage of protein synthesis emphasize this change in perception. This chapter focuses on how the information gathered principally since the last ribosome meeting has enhanced one's understanding of the termination phase of protein synthesis. RF3 has been shown to enhance the efficiency of decoding of stop signals and in particular the signals that are used by highly expressed genes. This suggests that when bacteria require high rates of translation and efficient decoding of stop signals, RF3 makes an important contribution to the translational efficiency. The structure of IF1 has been determined by nuclear magnetic resonance spectroscopy and is classified as a member of an oligomer binding (OB)-fold family of proteins, based on the ability of this structure to bind oligosaccharides and oligonucleotides. The discovery of recoding provided examples of stop codons regularly failing to terminate protein synthesis, such as at the RF2 frameshift site. The discovery that RF3 was a translational G protein was puzzling, considering early work which examined the effect of guanine nucleotides on RF3 activity. The disassembly of the termination complex in prokaryotes was shown almost 30 years ago to involve two factors, a ribosome-releasing factor, now called ribosome-recycling factor (RRF), and EF-G.