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Telomerase and the chromosome end replication problem

T R Cech¹, J Lingner

¹Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215, USA.

Ciba Foundation Symposium

|January 1, 1997

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Researchers purified telomerase, an enzyme crucial for DNA replication, from Euplotes aediculatus. This enzyme requires a specific DNA tail, suggesting a multi-step process for telomere replication in eukaryotes.

Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Telomerase is essential for maintaining chromosomal ends (telomeres) in eukaryotes.
Hypotrichous ciliates like Euplotes aediculatus are rich in telomeres and telomerase due to numerous short DNA molecules.
Telomerase comprises RNA and protein subunits, with significant variation in RNA sequences across species.

Purpose of the Study:

To investigate the structure and function of telomerase in Euplotes aediculatus.
To identify the protein subunits of Euplotes aediculatus telomerase.
To understand the primer requirements for telomerase activity.

Main Methods:

Cloning and sequencing of telomerase RNA subunits from ciliates.
Affinity chromatography using the RNA subunit to purify telomerase.

Related Experiment Videos

Biochemical assays to determine telomerase activity with different DNA primers.

Main Results:

Euplotes aediculatus telomerase RNA subunits share a common secondary structure despite low sequence homology.
Two protein subunits (123 kDa and 43 kDa) were identified in the purified enzyme.
A yeast homologue was found for the 123 kDa subunit, suggesting conserved protein components.
Purified telomerase requires a 4-6 nucleotide single-stranded 3' DNA tail for activity, not blunt ends.

Conclusions:

Telomerase protein subunits may be more evolutionarily conserved than RNA subunits.
The primer requirement supports a model where other enzymes prepare DNA for telomerase extension.
This model of telomere replication may apply broadly across eukaryotic organisms.