Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Cell Line
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Cloning, Molecular
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DNA, Complementary / genetics
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism*
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Gene Expression
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Humans
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Molecular Sequence Data
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Deletion
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Telomere / genetics*
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Telomere / metabolism*
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Telomere-Binding Proteins*
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Telomeric Repeat Binding Protein 1
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Tissue Distribution
Substances
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DNA, Complementary
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DNA-Binding Proteins
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RNA, Messenger
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Recombinant Proteins
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TINF2 protein, human
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Telomere-Binding Proteins
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Telomeric Repeat Binding Protein 1