Abstract
The telomere ends of linear chromosomes are replicated by the riboprotein complex telomerase. Telomerase is a large riboprotein complex that uses an integral RNA template and a specialized reverse transcriptase to processively synthesize the G‐rich strand. Telomerase has only a low or undetectable level of activity in normal somatic cells, but is highly active in most cancers, and is thus of interest as a target for anticancer drugs. The RNA component of telomerase plays an integral role in catalysis, localization, and processing. Results on the structure of domains of the RNA component of human telomerase, and how mutations in the RNA affect the structure and function of telomerase, will be presented. These domains include a pseudoknot containing a catalytically essential triple helical region and an H/ACA domain. Related results on H/ACA snoRNAs involved in pseudouridylation will be presented.
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