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Protein-RNA interaction restricts telomerase from running through the stop sign

Nature Structural & Molecular Biology volume 22, pages 835–836 (2015)Cite this article

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Telomerase is a unique reverse transcriptase in that it repetitively uses a short piece of its RNA component as template to synthesize DNA. A new crystal structure of a part of the Tetrahymena telomerase ribonucleoprotein reveals how reverse transcription is limited to this specific template region.

Telomerase is a ribonucleoprotein (RNP) complex that adds telomeric DNA repeats to chromosome ends, thus compensating for the attrition that occurs due to incomplete DNA replication. Its catalytic core is composed of two key components: telomerase RNA (TER) and telomerase reverse transcriptase (TERT)1,2. Unlike other reverse transcriptases, which move along their templates and reverse-transcribe the entire RNA sequence, TERT uses only a small segment of TER as template and translocates between the beginning and end of this template region to synthesize repetitive sequences. In various species, a template boundary element (TBE) on TER has been shown to be essential to keep the catalytic site of TERT from reverse-transcribing beyond the template region3,4,5,6. In this issue, Jansson et al.7 report the 3-Å crystal structure of the Tetrahymena telomerase RNA-binding domain (tTRBD) in complex with the TBE RNA, revealing the detailed interactions at this protein-RNA surface and demonstrating the structural basis of template-boundary definition.

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Figure 1: Hypothesized evolutionary path of biocatalysis.
Figure 2: Comparison between telomerase and other reverse transcriptases.
Figure 3: Location of the TBE in TER and the TRBD in the TERT protein.

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  1. Linghe Xi and Thomas R. Cech are at the Department of Molecular, Cellular and Developmental Biology, BioFrontiers Institute, and the Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado, USA.,

    Linghe Xi & Thomas R Cech

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  1. Linghe Xi
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Correspondence to Thomas R Cech.

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Thomas R. Cech is on the Board of Directors of Merck, Inc.

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Xi, L., Cech, T. Protein-RNA interaction restricts telomerase from running through the stop sign. Nat Struct Mol Biol 22, 835–836 (2015). https://doi.org/10.1038/nsmb.3118

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