Publication details
Human Telomere Repeat Binding Factor TRF1 Replaces TRF2 Bound to Shelterin Core Hub TIN2 when TPP1 Is Absent
| Authors | |
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| Year of publication | 2020 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | Telomeric repeat binding factor TRF1, TRF2 together with TIN2 protein create important roles as a shelterin-core subunits. Their dynamics is important for regulating the assembly of shelterin complex. We applied FCCS – Fluorescence Cross-Correlation Spectroscopy as an in vitro single molecule fluorescence microscopy approach to quantitatively describe the exchange of TRF1 and TRF2 in complex of TIN2. We found that TRF1 can effectively exchange TRF2 in TIN2-TRF2 complex which is essential regarding the function of shelterin during specific recognition of chromosome ends and telomerase activity regulation. We extended the FCCS study with addition of TPP1 which is TIN2 binding partner and tested whether TPP1 presence could change the TIN2-TRF2 interaction and enable TIN2 interact simultaneously with TRF1 and TRF2, hence allow to originate TRF1-TIN2- TRF2 shelterin-core complex. Our FCCS data shows that TPP1 indeed upon binding to TIN2 induce allosteric effect improving the binding capacity so the complex TPP1-TIN2 can accommodate both TRF1 and TRF2 and it is essential for the proper formation of TRF1-TIN2-TRF2 shelterin-core complex. |
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