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First published online 2 October 2007
doi: 10.1242/jcs.004119


Journal of Cell Science 120, 3678-3687 (2007)
Published by The Company of Biologists 2007
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Research Article

Arabidopsis POT1A interacts with TERT-V(I8), an N-terminal splicing variant of telomerase

Pascale Rossignol, Sarah Collier, Max Bush, Peter Shaw and John H. Doonan*

Department of Cellular and Developmental Biology, John Innes Centre, Norwich, NR4 7UH, UK

* Author for correspondence (e-mail: john.doonan{at}bbsrc.ac.uk)

Accepted 21 August 2007

Chromosome integrity is maintained via the actions of ribonucleoprotein complexes that can add telomeric repeats or can protect the chromosome end from being degraded. POT1 (protection of telomeres 1), a class of single-stranded-DNA-binding proteins, is a regulator of telomeric length. The Arabidopsis genome contains three POT1 homologues: POT1A, POT1B and POT1C. Using yeast two-hybrid assays to identify components of a potential POT1A complex, we retrieved three interactors: the N-terminus of the telomerase, a protein kinase and a plant-specific protein. Further analysis of the interaction of POT1 proteins with telomerase showed that this interaction is specific to POT1A, suggesting a specific role for this paralogue. The interaction is specific to the N-terminal region of the telomerase, which can be encoded by splicing variants. This interaction indicates possible mechanisms for telomerase regulation by alternative splicing and by POT1 proteins.

Key words: Telomere, Protein-protein interaction


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