Inhibition of lagging strand replication by G-rich telomeric DNA and the shelterin subunit POT1
Leonard-Booker C +6 more
europepmc +1 more source
The POT1–TPP1 telomere complex is a telomerase processivity factor [PDF]
Telomeres were originally defined as chromosome caps that prevent the natural ends of linear chromosomes from undergoing deleterious degradation and fusion events. POT1 (protection of telomeres) protein binds the single-stranded G-rich DNA overhangs at human chromosome ends and suppresses unwanted DNA repair activities.
Feng Wang +2 more
exaly +5 more sources
The N Terminus of the OB Domain of Telomere Protein TPP1 Is Critical for Telomerase Action [PDF]
Telomerase recruitment to telomeres and enzymatic processivity are mediated by TPP1, an essential component of telomere integrity and telomerase function. A surface on the OB domain of TPP1 called the TEL patch is critical for TPP1's telomerase-associated functions.
Sherilyn Grill +2 more
exaly +5 more sources
POT1-TPP1 telomere length regulation and disease [PDF]
Telomeres are DNA repeats at the ends of linear chromosomes and are replicated by telomerase, a ribonucleoprotein reverse transcriptase. Telomere length regulation and chromosome end capping are essential for genome stability and are mediated primarily by the shelterin and CST complexes.
, Emmanuel Skordalakes
exaly +6 more sources
Multiple facets of TPP1 in telomere maintenance [PDF]
Telomeres are nucleoprotein complexes that cap the ends of all linear chromosomes and function to prevent aberrant repair and end-to-end chromosome fusions. In somatic cells, telomere shortening is a natural part of the aging process as it occurs with each round of cell division.
Malligarjunan Rajavel, Derek J Taylor
exaly +3 more sources
POT1-TPP1 binding stabilizes POT1, promoting efficient telomere maintenance
Telomeric POT1-TPP1 binding is critical to telomere maintenance and disruption of this complex may lead to cancer. Current data suggests a reduction of intracellular POT1 levels in the absence of TPP1. Here we provide evidence of POT1 plasticity that contributes to its lack of stability in the absence of TPP1 binding. Structural data reveals inter- and
, Cory Rice, Emmanuel Skordalakes
exaly +4 more sources
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Structural basis of human telomerase recruitment by TPP1-POT1
Science, 2022Telomerase maintains genome stability by extending the 3′ telomeric repeats at eukaryotic chromosome ends, thereby counterbalancing progressive loss caused by incomplete genome replication. In mammals, telomerase recruitment to telomeres is mediated by TPP1, which assembles as a heterodimer with POT1.
Zala Sekne +3 more
openaire +2 more sources
TPP1 Inhibits DNA Damage Response and Chemosensitivity in Esophageal Cancer
Critical Reviews in Eukaryotic Gene Expression, 2023TPP1, as one of the telomere-protective protein complex, functions to maintain telomere stability. In this study, we found that TPP1 was significantly upregulated in esophageal cancer (EC). We found that the proliferation and migration ability were significantly inhibited, while the results of flow cytometry assay indicated that the growth was hindered
Jilin, Wen +10 more
exaly +3 more sources
Telomere protection by mammalian Pot1 requires interaction with Tpp1
Nature Structural & Molecular Biology, 2007The shelterin complex at mammalian telomeres contains the single-stranded DNA-binding protein Pot1, which regulates telomere length and protects chromosome ends. Pot1 binds Tpp1, the shelterin component that connects Pot1 to the duplex telomeric DNA-binding proteins Trf1 and Trf2.
Dirk, Hockemeyer +8 more
openaire +2 more sources
The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment [PDF]
The shelterin protein TPP1 is involved in both recruiting telomerase and stimulating telomerase processivity in human cells. Assessing the in vivo significance of the latter role of TPP1 has been difficult, because TPP1 mutations that perturb telomerase ...
Ranjodh Sandhu +2 more
exaly +2 more sources

