西亚试剂：Common chaperone activity in the G-domain of trGTPase prote

protects L11–L12 interaction on the ribosome

Dandan Zhang, Guangqiao Liu, Jiaying Xue, Jizhong Lou, Knud H. Nierhaus, Weimin Gong and Yan Qin

Translational GTPases (trGTPases) regulate all phases of protein synthesis. An early event in the interaction of a trGTPase with the ribosome is the contact of the G-domain with the C-terminal domain (CTD) of ribosomal protein L12 (L12-CTD) and subsequently interacts with the N-terminal domain of L11 (L11-NTD). However, the structural and functional relationships between L12-CTD and L11-NTD remain unclear. Here, we performed mutagenesis, biochemical and structural studies to identify the interactions between L11-NTD and L12-CTD. Mutagenesis of conserved residues in the interaction site revealed their role in the docking of trGTPases. During docking, loop62 of L11-NTD protrudes into a cleft in L12-CTD, leading to an open conformation of this domain and exposure of hydrophobic core. This unfavorable situation for L12-CTD stability is resolved by a chaperone-like activity of the contacting G-domain. Our results suggest that all trGTPases—regardless of their different specific functions—use a common mechanism for stabilizing the L11-NTD.L12-CTD interactions.

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