You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Functional importance of telomerase pseudoknot revealed by single-molecule analysis
Mariana Mihalusova, John Y. Wu and Xiaowei Zhuang
Proceedings of the National Academy of Sciences of the United States of America
Vol. 108, No. 51 (December 20, 2011), pp. 20339-20344
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/23077247
Page Count: 6
You can always find the topics here!Topics: RNA, Enzymes, Nucleotides, Histograms, Genetic mutation, Molecules, Dyes, Trajectories, Catalysis, Imaging
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Preview not available
Telomerase ribonucleoprotein (RNP) employs an RNA subunit to template the addition of telomeric repeats onto chromosome ends. Previous studies have suggested that a region of the RNA downstream of the template may be important for telomerase activity and that the region could fold into a pseudoknot. Whether the pseudoknot motif is formed in the active telomerase RNP and what its functional role is have not yet been conclusively established. Using single-molecule FRET, we show that the isolated pseudoknot sequence stably folds into a pseudoknot. However, in the context of the full-length telomerase RNA, interference by other parts of the RNA prevents the formation of the pseudoknot. The protein subunits of the telomerase holoenzyme counteract RNA-induced misfolding and allow a significant fraction of the RNPs to form the pseudoknot structure. Only those RNP complexes containing a properly folded pseudoknot are catalytically active. These results not only demonstrate the functional importance of the pseudoknot but also reveal the critical role played by telomerase proteins in pseudoknot folding.
Proceedings of the National Academy of Sciences of the United States of America © 2011 National Academy of Sciences