Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein

Michael D. Stone, Mariana Mihalusova, Catherine M. O’Connor, Ramadevi Prathapam, Kathleen Collins and Xiaowei Zhuang ()
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Michael D. Stone: Department of Chemistry and Chemical Biology,
Mariana Mihalusova: Department of Molecular and Cellular Biology,
Catherine M. O’Connor: University of California, Berkeley, California 94720, USA
Ramadevi Prathapam: University of California, Berkeley, California 94720, USA
Kathleen Collins: University of California, Berkeley, California 94720, USA
Xiaowei Zhuang: Department of Chemistry and Chemical Biology,

Nature, 2007, vol. 446, issue 7134, 458-461

Abstract: How telomerase shapes up The biogenesis of telomerase, the ribonucleoprotein (RNP) assembly that stabilizes the termini of linear chromosomes, is an important process in a healthy cell and mutations that disrupt it cause disease. Mechanisms of RNP assembly are poorly understood. Michael Stone et al. have used a single-molecule approach to examine telomerase assembly in real time. The results establish an assembly mechanism featuring successive steps of protein-induced RNA folding, ultimately moulding the telomerase complex into its functional shape.

Date: 2007
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DOI: 10.1038/nature05600

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