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Our structural snapshots were complemented by kinetic studies, allowing us to understand how telomerase chooses right from wrong nucleotides; that is, selecting canonical dNTPs with correct base pairing compared to noncanonical rNTPs or mismatched base pairing (Figure 6A). Our experiments were carried out specifically with a single dGTP insertion using a 4 nucleotide overhang RNA template. While telomerase has been shown to exhibit moderate base and position-specific effects, our results indicate that the telomerase catalytic core generally exhibits moderate base selection fidelity, similar to that of X-family polymerases involved in DNA repair (Chen et al, 2021; McCulloch and Kunkel, 2008). Based on our kinetic values, we predict that telomerase inserts ~ 1 mismatch per each 10 kb of telomere extension. Because telomerase does not have a proofreading domain, misinsertions created by telomerase will remain as ssDNA during telomere elongation. Upon replication of the complementary strands by a DNA polymerase, the base that was a mismatch (in the context of telomerase) will become a matched base pair, and will not be a substrate for mismatch repair. Therefore, our fidelity measurement is predictive of cellular error rates in telomeric sequences. Accordingly, our predicted error rate agrees with telomeric error rates observed using telomere sequencing (Lee et al, 2021). While the downstream consequences of telomeric mismatches have not been studied in a biological context to our knowledge, they likely would disrupt G-quadruplex stability and inhibit shelterin protein binding, as both of these phenomena are dependent on DNA sequence (Figure 6B; Burge et al, 2006; de Lange, 2005).