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Annu Rev Biophys. 2017 Mar 15. doi: 10.1146/annurev-biophys-062215-011140. [Epub ahead of print]

Progress in Human and Tetrahymena Telomerase Structure.

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1
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569; email: feigon@uclaue.mbi.ucla.edu , henrychan106@ucla.edu , and yaqiang@mbi.ucla.edu.

Abstract

Telomerase is an RNA-protein complex that extends the 3' ends of linear chromosomes, using a unique telomerase reverse transcriptase (TERT) and template in the telomerase RNA (TR), thereby helping to maintain genome integrity. TR assembles with TERT and species-specific proteins, and telomerase function in vivo requires interaction with telomere-associated proteins. Over the past two decades, structures of domains of TR and TERT as well as other telomerase- and telomere-interacting proteins have provided insights into telomerase function. A recently reported 9-Å cryo-electron microscopy map of the Tetrahymena telomerase holoenzyme has provided a framework for understanding how TR, TERT, and other proteins from ciliate as well as vertebrate telomerase fit and function together as well as unexpected insight into telomerase interaction at telomeres. Here we review progress in understanding the structural basis of human and Tetrahymena telomerase activity, assembly, and interactions. Expected final online publication date for the Annual Review of Biophysics Volume 46 is May 20, 2017. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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