This review summarizes our current understanding of translation in prokaryotes, focusing on
the mechanistic and structural aspects of each phase of translation: initiation, elongation …

The high-resolution structures of ribosomal subunits published in 2000 have revolutionized
the field of protein translation. They facilitated the determination and interpretation of …

The publication of crystal structures of the 50S and 30S ribosomal subunits and the intact
70S ribosome is revolutionizing our understanding of protein synthesis. This review is an …

Structures of the bacterial ribosome have provided a framework for understanding universal
mechanisms of protein synthesis. However, the eukaryotic ribosome is much larger than it is …

▪ Abstract Great advances have been made in the past three decades in understanding the
molecular mechanics underlying protein synthesis in bacteria, but our understanding of the …

Termination of protein synthesis is not 100% efficient. A number of natural mechanisms that
suppress translation termination exist. One of them is STOP codon readthrough, the process …

The Escherichia coli relBE operon encodes a toxin-antitoxin pair, RelE-RelB. RelB can
reverse inhibition of protein synthesis by RelE in vivo. We have found that although RelE …

After termination, eukaryotic 80S ribosomes remain associated with mRNA, P-site
deacylated tRNA, and release factor eRF1 and must be recycled by dissociating these …

During the ribosomal translocation, the binding of elongation factor G (EF-G) to the
pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the …

Eukaryotic translation termination is triggered by peptide release factors eRF1 and eRF3.
Whereas eRF1 recognizes all three termination codons and induces hydrolysis of peptidyl …