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Vol. 13, No. 9, pp. 1116-1125, May 1, 1999
Division of Biochemistry and Molecular Biology, Department of
Molecular and Cell Biology, University of California, Berkeley,
Berkeley, California 94720-3204 USA
Telomerase is a ribonucleoprotein reverse transcriptase specialized
for use of a sequence within its integral RNA component as the template
for DNA synthesis. Telomerase adds telomeric simple sequence repeats to
single-stranded primers in vitro or chromosome ends in vivo. We have
investigated the sequences and structures of recombinant
Tetrahymena thermophila telomerase RNA necessary for physical
association and activity with the catalytic protein subunit expressed
in rabbit reticulocyte lysate. In contrast with previous results using
another reconstitution method, we find that phylogenetically conserved
primary sequences and a phylogenetically nonconserved secondary
structure are essential for telomerase RNA function. Telomerase RNA
binding to the catalytic protein subunit requires sequences 5' of
the template and is highly sequence specific. Other telomerase RNA
sequences are required for enzyme activity and proper template use but
not for protein interaction affinity. In addition, we demonstrate that
the production of active recombinant telomerase requires a factor in
rabbit reticulocyte lysate that promotes ribonucleoprotein assembly.
These studies demonstrate multiple functions for the telomerase RNA and
indicate that recombinant telomerase activity requires more than the
catalytic protein and RNA components of the enzyme that have been
identified to date.
[Key Words: telomerase; RNA; telomere; ribonucleoprotein; polymerase]
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