Journal
NUCLEIC ACIDS RESEARCH
Volume 46, Issue 16, Pages 8651-8661Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gky651
Keywords
-
Categories
Funding
- Leo Pharma Research Foundation
- Novo Nordisk Foundation
- Danish Council for Independent Research (Natural Sciences)
- National Institutes of Health [R01-GM080376, R35-GM118139]
- American Heart Association Postdoctoral Fellowship [12POST8910014]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM080376, R35GM118139] Funding Source: NIH RePORTER
Ask authors/readers for more resources
The GTPase elongation factor EF-Tu delivers aminoacyl-tRNAs to the mRNA-programmed ribosome during translation. Cognate codon-anticodon interaction stimulates GTP hydrolysis within EF-Tu. It has been proposed that EF-Tu undergoes a large conformational change subsequent to GTP hydrolysis, which results in the accommodation of aminoacyl-tRNA into the ribosomal A-site. However, this proposal has never been tested directly. Here, we apply single-molecule total internal reflection fluorescence microscopy to study the conformational dynamics of EF-Tu when bound to the ribosome. Our studies show that GTP hydrolysis initiates a partial, comparatively small conformational change of EF-Tu on the ribosome, not directly along the path from the solution 'GTP' to the 'GDP' structure. The final motion is completed either concomitant with or following dissociation of EF-Tu from the ribosome. The structural transition of EF-Tu on the ribosome is slower when aa-tRNA binds to a cognate versus a near-cognate codon. The resulting longer residence time of EFTu on the ribosome may be important for promoting accommodation of the cognate aminoacyl-tRNA into the A-site.
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