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Significance The telomerase enzyme is recruited to chromosome ends by telomeric protein TPP1 to replenish DNA that is lost during DNA replication. Although telomerase is not expressed in most of our cells, its presence is key to the continued division of stem cells and is exploited by a majority of cancers for their growth. Here, we used chimeras of mouse and human telomerase to define the regions necessary for interacting with TPP1. We then employed a multilayered, site-directed mutagenesis screen to reveal finer details of the surface that human telomerase uses to bind TPP1. Combining our data with the previously mapped interaction surface on TPP1, we present a functionally validated structural model for the human telomerase–TPP1 interaction.

Combining conservation and species-specific differences to determine how human telomerase binds telomeres