Molecular dissection of the silkworm ribosomal stalk complex: the role of multiple copies of the stalk proteins.

ABSTRACT: In animal ribosomes, two stalk proteins P1 and P2 form a heterodimer, and the two dimers, with the anchor protein P0, constitute a pentameric complex crucial for recruitment of translational GTPase factors to the ribosome. To investigate the functional contribution of each copy of the stalk proteins, we constructed P0 mutants, in which one of the two C-terminal helices, namely helix I (N-terminal side) or helix II (C-terminal side) were unable to bind the P1-P2 dimer. We also constructed 'one-C-terminal domain (CTD) stalk dimers', P1-P2ΔC and P1ΔC-P2, composed of intact P1/P2 monomer and a CTD-truncated partner. Through combinations of P0 and P1-P2 variants, various complexes were reconstituted and their function tested in eEF-2-dependent GTPase and eEF-1α/eEF-2-dependent polyphenylalanine

SUBMITTER: Baba K 

PROVIDER: S-EPMC3616719 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature