Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 21, Pages 10851-10865Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks833
Keywords
-
Categories
Funding
- Major State Basic Research of China 973 [2012CB911001, 2011CB910503]
- National Natural Science Foundation of China [31170756, 31270847, 31021062]
- Novo Nordisk Chinese Academy of Sciences Research Foundation
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available