Telomeres are DNA-protein structures that cap linear chromosomes and are essential for maintaining genomic stability and cell phenotype. We identified a novel human telomere-associated protein, TIN2, by interaction cloning using the telomeric DNA-binding-protein TRF1 as a bait. TIN2 interacted with TRF1 in vitro and in cells, and co-localized with TRF1 in nuclei and metaphase chromosomes. A mutant TIN2 that lacks amino-terminal sequences effects elongated human telomeres in a telomerase-dependent manner. Our findings suggest that TRF1 is insufficient for control of telomere length in human cells, and that TIN2 is an essential mediator of TRF1 function.
Pubmed ID: 10581025 RIS Download
Mesh terms: Amino Acid Sequence | Base Sequence | Cell Line | Cloning, Molecular | DNA, Complementary | DNA-Binding Proteins | Gene Expression | Humans | Molecular Sequence Data | RNA, Messenger | Recombinant Proteins | Sequence Deletion | Telomere | Telomere-Binding Proteins | Telomeric Repeat Binding Protein 1 | Tissue Distribution
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