TY - JOUR
T1 - Telomerase
T2 - What are the Est proteins doing?
AU - Taggart, Andrew K.P.
AU - Zakian, Virginia A.
N1 - Funding Information:
We thank Tim Fisher, Jean-Baptiste Boulé, Lara Goudsouzian, and Letty Vega for critical reading of the manuscript. Work in the Zakian laboratory is supported by grants from the National Institutes of Health. AKP Taggart was supported by National Institutes of Health grant T32 CA09528-16.
PY - 2003/6
Y1 - 2003/6
N2 - Saccharomyces cerevisiae has proven to be a useful model organism for the study of telomerase, a specialized cellular reverse transcriptase that helps maintain genomic stability by adding telomeric DNA repeats to the ends of chromosomes. Yeast telomerase is thought to be a holoenzyme containing Est2p and TLC1 RNA, the catalytic subunit and its intrinsic template, respectively, as well as the TLC1-RNA-associated factors Est1p and Est3p. Cdc13p, a sequence-specific telomere-DNA-binding protein, is also required for action in vivo. A current model for telomerase regulation is that telomere-associated Cdc13p binds Est1p, thereby recruiting telomerase. However, recent chromatin immunoprecipitation experiments suggest an alternate role for Est1p in activating Est2p-TLC1-RNA that is already bound to the telomere. Three models for Est1p activation are presented.
AB - Saccharomyces cerevisiae has proven to be a useful model organism for the study of telomerase, a specialized cellular reverse transcriptase that helps maintain genomic stability by adding telomeric DNA repeats to the ends of chromosomes. Yeast telomerase is thought to be a holoenzyme containing Est2p and TLC1 RNA, the catalytic subunit and its intrinsic template, respectively, as well as the TLC1-RNA-associated factors Est1p and Est3p. Cdc13p, a sequence-specific telomere-DNA-binding protein, is also required for action in vivo. A current model for telomerase regulation is that telomere-associated Cdc13p binds Est1p, thereby recruiting telomerase. However, recent chromatin immunoprecipitation experiments suggest an alternate role for Est1p in activating Est2p-TLC1-RNA that is already bound to the telomere. Three models for Est1p activation are presented.
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U2 - 10.1016/S0955-0674(03)00040-1
DO - 10.1016/S0955-0674(03)00040-1
M3 - Review article
C2 - 12787768
AN - SCOPUS:0038360921
VL - 15
SP - 275
EP - 280
JO - Current Opinion in Cell Biology
JF - Current Opinion in Cell Biology
SN - 0955-0674
IS - 3
ER -