The shelterin component TRF2 mediates columnar stacking of human telomeric chromatin

ABSTRACT: Telomere repeat binding factor 2 (TRF2) is an essential component of the telomeres and also plays an important role in a number of other non-telomeric processes. Detailed knowledge of the binding and interaction of TRF2 with telomeric nucleosomes is limited. Here, we study the binding of TRF2 to in vitro-reconstituted kilobasepair-long human telomeric chromatin fibres using electron microscopy, single-molecule force spectroscopy and analytical ultracentrifugation sedimentation velocity. Our electron microscopy results revealed that full-length and N-terminally truncated TRF2 promote the formation of a columnar structure of the fibres with an average width and compaction larger than that induced by the addition of Mg2+, in agreement with the in vivo observations. Single-molecule force spect

SUBMITTER: Dr. Sook Yi Wong 

PROVIDER: S-SCDT-10_1038-S44318-023-00002-3 | biostudies-other |

REPOSITORIES: biostudies-other