Svetlana Dokudovskaya

Telomerase from Saccharomyces cerevisiae contains several protein subunits and may have different activities depending on the protein content

Telomerase is a ribonucleoprotein responsible for maintaining telomeres during the cell cycle [1, 2]. Here we describe a two‐step purification procedure for the Saccharomyces cerevisiae telomerase complex. We have found that the properties (processivity, nuclease activity) of telomerase depend on the isolation procedure. Using a cross‐linking approach, we have revealed several proteins that could be components of the telomerase complex. Furthermore, spectra of cross‐linked proteins differ in processive and non‐processive telomerase complexes.

Comprehensive analysis of telomerase inhibition by gallotannin

Gallotannin (or tannic acid) is a naturally occurring compound that inhibits cell growth and activity of different DNA-polymerases, including telomerase. The purpose of the present study was to gain insight into the mechanism of telomerase inhibition by gallotannin. We determined that gallotannin inhibits telomerase in vitro with an half maximal inhibitory concentrations value of 130 nM, but it does not affect telomerase complex assembly and component levels in vivo. The inhibitory activity of gallotannin against telomerase provides an additional explanation for the anti-cancer activities of this compound.