Access
To read this story in full you will need to login or make a payment (see right).
Letter
Nature 446, 458-461 (22 March 2007) | doi:10.1038/nature05600; Received 18 September 2006; Accepted 15 January 2007; Published online 25 February 2007
Open Innovation Challenges
-
Novel Approaches to Protecting Maize from Insect Damage
The Seeker is looking for novel approaches to protecting maize from insect damage. This Challenge re...
-
Methods of Modeling Adaptation in Populations
The analysis of adaptation with a population is a frequently encountered computational modeling scen...
nature jobs
Senior Scientific Manager / Chief Scientific Manager for Metabolic Disorder and Cardiavascular Area In Vivo Pharmacology / Biology
- Syngene International
- Bangalore, Karnataka 560099 India
System Engineer (Simulation and Modelling)
- Praj Matrix - Praj Industries Ltd
- Pune, Maharashtra Pune-411021 India
Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein
Michael D. Stone1, Mariana Mihalusova2, Catherine M. O'Connor5, Ramadevi Prathapam5, Kathleen Collins5 & Xiaowei Zhuang1,3,4
- Department of Chemistry and Chemical Biology,
- Department of Molecular and Cellular Biology,
- Department of Physics, and,
- Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138, USA
- Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA
Correspondence to: Xiaowei Zhuang1,3,4 Correspondence and requests for materials should be addressed to X.Z. (Email: zhuang@chemistry.harvard.edu).
Abstract
Telomerase is an essential cellular ribonucleoprotein (RNP) that solves the end replication problem and maintains chromosome stability by adding telomeric DNA to the termini of linear chromosomes1, 2, 3. Genetic mutations that abrogate the normal assembly of telomerase RNP cause human disease4. It is therefore of fundamental and medical importance to decipher cellular strategies for telomerase biogenesis, which will require new insights into how specific interactions occur in a precise order along the RNP assembly pathway. Here we use a single-molecule approach to dissect the individual assembly steps of telomerase. Direct observation of complex formation in real time revealed two sequential steps of protein-induced RNA folding, establishing a hierarchical RNP assembly mechanism: interaction with the telomerase holoenzyme protein p65 induces structural rearrangement of telomerase RNA, which in turn directs the binding of the telomerase reverse transcriptase to form the functional ternary complex. This hierarchical assembly process is facilitated by an evolutionarily conserved structural motif within the RNA. These results identify the RNA folding pathway during telomerase biogenesis and define the mechanism of action for an essential telomerase holoenzyme protein.
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
La sets the tone for telomerase assemblyNature Structural & Molecular Biology News and Views (01 Apr 2007)
RESEARCH
A telomerase holoenzyme protein enhances telomerase RNA assembly with telomerase reverse transcriptaseNature Structural & Molecular Biology Article (01 Mar 2005)
Structure of stem-loop IV of Tetrahymena telomerase RNAThe EMBO Journal Article (12 Jul 2006)
Triple-helix structure in telomerase RNA contributes to catalysisNature Structural & Molecular Biology Article (01 Jun 2008)
See all 25 matches for Research
