Journal
EMBO REPORTS
Volume 18, Issue 2, Pages 280-291Publisher
WILEY
DOI: 10.15252/embr.201642548
Keywords
electron microscopy; Elongator; structure; tRNA modification
Categories
Funding
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN 418157-2012]
- Michael Smith Foundation for Health Research Career Investigator Award
- Canadian Institutes of Health Research (CIHR) New Investigator Award
- Canadian Foundation for Innovation (CFI)
- NSERC CGS fellowship
Ask authors/readers for more resources
Elongator is a 850 kDa protein complex involved in multiple processes from transcription to tRNA modification. Conserved from yeast to humans, Elongator is assembled from two copies of six unique subunits (Elp1 to Elp6). Despite the wealth of structural data on the individual subunits, the overall architecture and subunit organization of the full Elongator and the molecular mechanisms of how it exerts its multiple activities remain unclear. Using single-particle electron microscopy (EM), we revealed that yeast Elongator adopts a bilobal architecture and an unexpected asymmetric subunit arrangement resulting from the hexameric Elp456 subassembly anchored to one of the two Elp123 lobes that form the structural scaffold. By integrating the EM data with available subunit crystal structures and restraints generated from cross-linking coupled to mass spectrometry, we constructed a multiscale molecular model that showed the two Elp3, the main catalytic subunit, are located in two distinct environments. This work provides the first structural insights into Elongator and a framework to understand the molecular basis of its multifunctionality.
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