Progress in structural studies of telomerase
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Updated: May 3, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase
Published on: July 14, 2011
Edward J Miracco1, Jiansen Jiang2, Darian D Cash1
1Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA.
Abstract:
Telomerase is the ribonucleoprotein (RNP) reverse transcriptase responsible for synthesizing the 3' ends of linear chromosomes. It plays critical roles in tumorigenesis, cellular aging, and stem cell renewal. The past two years have seen exciting progress in determining telomerase holoenzyme architecture and the structural basis of telomerase activity. Notably, the first electron microscopy structures of telomerase were reported, of the Tetrahymena thermophila telomerase holoenzyme and a human telomerase dimer. In addition to new structures of TERT and TER domains, the first structures of telomerase protein domains beyond TERT, and their complexes with TER or telomeric single-stranded DNA, were reported. Together these studies provide the first glimpse into the organization of the proteins and RNA in the telomerase RNP.
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