Journal
RNA
Volume 11, Issue 12, Pages 1898-1908Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.2192805
Keywords
ribosome dynamics; translation initiation; protein synthesis; chemical probing
Categories
Funding
- NIGMS NIH HHS [R01-GM65050, T32 GM066698, T32 GM007232, R01 GM065050, 1 T32 GM066698-01AI, T32-GM07232-27] Funding Source: Medline
Ask authors/readers for more resources
Protein biosynthesis requires numerous conformational rearrangements within the ribosome. The structural core of the ribosome is composed of RNA and is therefore dependent on counterions such as magnesium ions for function. Many steps of translation can be compromised or inhibited if the concentration of Mg2+ is too low or too high. Conditions previously used to probe the conformation of the mammalian ribosome in vitro used high Mg2+ concentrations that we find completely inhibit translation in vitro. We have therefore probed the conformation of the small ribosomal subunit in low concentrations of Mg2+ that support translation in vitro and compared it with the conformation of the 40S subunit at high Mg2+ concentrations. In low Mg2+ concentrations, we find significantly more changes in chemical probe accessibility in the 40S subunit due to subunit association or binding of the hepatitis C internal ribosomal entry site (HCV IRES) than had been observed before. These results suggest that the ribosome is more dynamic in its functional state than previously appreciated.
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