Structural highlights
Function
[EF1A_PYRHO] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] [RL12_PYRHO] Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. The stalk complex of P.horikoshii binds to E.coli large subunits and confers on them the ability to interact with eukaryotic elongation factors. Each succesive L12 dimer bound along the P0 spine increases the GTPase activity of elongation factors and increases translation by reconsituted ribosomes.[1]
Publication Abstract from PubMed
In all organisms, the large ribosomal subunit contains multiple copies of a flexible protein, the so-called 'stalk'. The C-terminal domain (CTD) of the stalk interacts directly with the translational GTPase factors, and this interaction is required for factor-dependent activity on the ribosome. Here we have determined the structure of a complex of the CTD of the archaeal stalk protein aP1 and the GDP-bound archaeal elongation factor aEF1alpha at 2.3 A resolution. The structure showed that the CTD of aP1 formed a long extended alpha-helix, which bound to a cleft between domains 1 and 3 of aEF1alpha, and bridged these domains. This binding between the CTD of aP1 and the aEF1alpha*GDP complex was formed mainly by hydrophobic interactions. The docking analysis showed that the CTD of aP1 can bind to aEF1alpha*GDP located on the ribosome. An additional biochemical assay demonstrated that the CTD of aP1 also bound to the aEF1alpha*GTP*aminoacyl-tRNA complex. These results suggest that the CTD of aP1 interacts with aEF1alpha at various stages in translation. Furthermore, phylogenetic perspectives and functional analyses suggested that the eukaryotic stalk protein also interacts directly with domains 1 and 3 of eEF1alpha, in a manner similar to the interaction of archaeal aP1 with aEF1alpha.
Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1alpha.,Ito K, Honda T, Suzuki T, Miyoshi T, Murakami R, Yao M, Uchiumi T Nucleic Acids Res. 2014 Dec 16;42(22):14042-52. doi: 10.1093/nar/gku1248. Epub, 2014 Nov 26. PMID:25428348[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maki Y, Hashimoto T, Zhou M, Naganuma T, Ohta J, Nomura T, Robinson CV, Uchiumi T. Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. J Biol Chem. 2007 Nov 9;282(45):32827-33. Epub 2007 Sep 5. PMID:17804412 doi:http://dx.doi.org/10.1074/jbc.M705412200
- ↑ Ito K, Honda T, Suzuki T, Miyoshi T, Murakami R, Yao M, Uchiumi T. Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1alpha. Nucleic Acids Res. 2014 Dec 16;42(22):14042-52. doi: 10.1093/nar/gku1248. Epub, 2014 Nov 26. PMID:25428348 doi:http://dx.doi.org/10.1093/nar/gku1248
