4beh
Solution structure of human ribosomal protein P1.P2 heterodimer
Structural highlights
FunctionRLA1_HUMAN Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478] Publication Abstract from PubMedLateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1*P2 heterodimers to form a P0(P1*P2)2 pentameric P-complex. Here, we have solved the structure of full-length P1*P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1*P2 are unstructured and can extend up to approximately 125 A away from the dimerization domains. 15N relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)4/L11 by eukaryotic P0(P1*P2)2/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS. Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.,Lee KM, Yusa K, Chu LO, Wing-Heng Yu C, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T Nucleic Acids Res. 2013 Jul 26. PMID:23892290[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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