
doi: 10.1242/jcs.004119
pmid: 17911168
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.
Cell Nucleus, Base Sequence, Arabidopsis Proteins, Molecular Sequence Data, Telomere-Binding Proteins, Arabidopsis, Nuclear Proteins, Telomere, Chromosomes, Plant, Shelterin Complex, Alternative Splicing, Catalytic Domain, Amino Acid Sequence, Telomerase
Cell Nucleus, Base Sequence, Arabidopsis Proteins, Molecular Sequence Data, Telomere-Binding Proteins, Arabidopsis, Nuclear Proteins, Telomere, Chromosomes, Plant, Shelterin Complex, Alternative Splicing, Catalytic Domain, Amino Acid Sequence, Telomerase
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