Nucleic Acids Research, Vol 26, Issue 6 1495-1502, Copyright © 1998 by Oxford University Press
NF Lue and J Xia
A gel mobility shift assay was developed to examine recognition of yeast
telomeres by telomerase. An RNase-sensitive G-rich strand- specific binding
activity can be detected in partially purified yeast telomerase fractions.
The binding activity was attributed to telomerase, because it co-purifies
with TLC1 RNA and telomerase activity over three different chromatographic
steps and because the complex co-migrates with TLC1 RNA when subjected to
electrophoresis through native gels. Analysis of the binding specificity of
yeast telomerase indicates that it recognizes the G-rich strand of yeast
telomeres with high affinity and specificity. The K d for the interaction
is approximately 3 nM. Single-stranded G-rich telomeres from other species,
such as human and Tetrahymena, though capable of being extended by yeast
telomerase in polymerization assays at high concentrations, bind the enzyme
with at least 100-fold lower affinities. The ability of a sequence to be
bound tightly by yeast telomerase in vitro correlates with its ability to
seed telomere formation in vivo. The implications of these findings for
regulation of telomerase activity are discussed.
ARTICLES
Species-specific and sequence-specific recognition of the dG-rich strand of telomeres by yeast telomerase
Department of Microbiology, W. R. Hearst Microbiology Research Center, Cornell University Medical College, 1300 York Avenue, New York, NY 10021, USA. nflue@mail.med.cornell.edu
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