1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.

The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones.

Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.

Elongation factor RbbA is required for ATP-dependent deacyl-tRNA release presumably after each peptide bond formation; however, there is no information about the cellular role. Proteomic analysis in Escherichia coli revealed that RbbA reciprocally co-purified with a conserved inner membrane protein of unknown function, YhjD. Both proteins are also physically associated with the 30S ribosome and with members of the lipopolysaccharide transport machinery.

The translation elongation factor eEF1B plays a role in the oxidative stress response pathway.

The multi-subunit guanine nucleotide exchange factor eEF1B for Saccharomyces cerevisiae Translation Elongation Factor 1A (eEF1A) has catalytic (eEF1Balpha) and noncatalytic (eEF1Bgamma) subunits. Deletion of the two nonessential genes encoding eEF1Bgamma has no dramatic effects on total protein synthesis or translational fidelity. Instead, loss of each gene gives resistance to oxidative stress, and loss of both is additive.