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JCS ePress online publication date 2 Oct 2007
doi: 10.1242/jcs.004119


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

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.




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