The architecture of Tetrahymena telomerase holoenzyme

Jiansen Jiang, Edward J. Miracco, Kyungah Hong, Barbara Eckert, Henry Chan, Darian D. Cash, Bosun Min, Z. Hong Zhou (), Kathleen Collins () and Juli Feigon ()
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Jiansen Jiang: Immunology and Molecular Genetics, University of California
Edward J. Miracco: University of California
Kyungah Hong: University of California
Barbara Eckert: University of California
Henry Chan: University of California
Darian D. Cash: University of California
Bosun Min: University of California
Z. Hong Zhou: Immunology and Molecular Genetics, University of California
Kathleen Collins: University of California
Juli Feigon: University of California

Nature, 2013, vol. 496, issue 7444, 187-192

Abstract: Abstract Telomerase adds telomeric repeats to chromosome ends using an internal RNA template and a specialized telomerase reverse transcriptase (TERT), thereby maintaining genome integrity. Little is known about the physical relationships among protein and RNA subunits within a biologically functional holoenzyme. Here we describe the architecture of Tetrahymena thermophila telomerase holoenzyme determined by electron microscopy. Six of the seven proteins and the TERT-binding regions of telomerase RNA (TER) have been localized by affinity labelling. Fitting with high-resolution structures reveals the organization of TERT, TER and p65 in the ribonucleoprotein (RNP) catalytic core. p50 has an unanticipated role as a hub between the RNP catalytic core, p75–p19–p45 subcomplex, and the DNA-binding Teb1. A complete in vitro holoenzyme reconstitution assigns function to these interactions in processive telomeric repeat synthesis. These studies provide the first view of the extensive network of subunit associations necessary for telomerase holoenzyme assembly and physiological function.

Date: 2013
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DOI: 10.1038/nature12062

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