Structural highlights
Function
[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] [RL10_PYRHO] Forms the large subunit's ribosomal stalk, playing a central role in the interaction of the ribosome with elongation 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, although the first site is the most stimulatory.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The archaeal ribosomal stalk complex has been shown to have an apparently conserved functional structure with eukaryotic pentameric stalk complex; it provides access to eukaryotic elongation factors at levels comparable to that of the eukaryotic stalk. The crystal structure of the archaeal heptameric (P0(P1)(2)(P1)(2)(P1)(2)) stalk complex shows that the rRNA anchor protein P0 consists of an N-terminal rRNA-anchoring domain followed by three separated spine helices on which three P1 dimers bind. Based on the structure, we have generated P0 mutants depleted of any binding site(s) for P1 dimer(s). Factor-dependent GTPase assay of such mutants suggested that the first P1 dimer has higher activity than the others. Furthermore, we constructed a model of the archaeal 50 S with stalk complex by superposing the rRNA-anchoring domain of P0 on the archaeal 50 S. This model indicates that the C termini of P1 dimers where translation factors bind are all localized to the region between the stalk base of the 50 S and P0 spine helices. Together with the mutational experiments we infer that the functional significance of multiple copies of P1 is in creating a factor pool within a limited space near the stalk base of the ribosome.
Structural basis for translation factor recruitment to the eukaryotic/archaeal ribosomes.,Naganuma T, Nomura N, Yao M, Mochizuki M, Uchiumi T, Tanaka I J Biol Chem. 2010 Feb 12;285(7):4747-56. Epub 2009 Dec 10. PMID:20007716[3]
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
- ↑ 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
- ↑ Naganuma T, Nomura N, Yao M, Mochizuki M, Uchiumi T, Tanaka I. Structural basis for translation factor recruitment to the eukaryotic/archaeal ribosomes. J Biol Chem. 2010 Feb 12;285(7):4747-56. Epub 2009 Dec 10. PMID:20007716 doi:10.1074/jbc.M109.068098
