The structural biology of the shelterin complex
- PMID: 30352022
- DOI: 10.1515/hsz-2018-0368
The structural biology of the shelterin complex
Abstract
The shelterin complex protects telomeric DNA and plays critical roles in maintaining chromosome stability. The structures and functions of the shelterin complex have been extensively explored in the past decades. This review summarizes the current progress on structural studies of shelterin complexes from different species. It focuses on the structural features and assembly of common structural domains, highlighting the evolutionary plasticity and conserved roles of shelterin proteins in telomere homeostasis and protection.
Keywords: DNA binding; protein-protein interaction; shelterin complex; structural biology; telomere; telomeric protein.
References
-
- Azad, G.K. and Tomar, R.S. (2016). The multifunctional transcription factor Rap1: a regulator of yeast physiology. Front Biosci. 21, 918–930.
-
- Baumann, P. and Cech, T.R. (2001). Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171–1175.
-
- Benarroch-Popivker, D., Pisano, S., Mendez-Bermudez, A., Lototska, L., Kaur, P., Bauwens, S., Djerbi, N., Latrick, C.M., Fraisier, V., Pei, B., et al. (2016). TRF2-mediated control of telomere DNA topology as a mechanism for chromosome-end protection. Mol. Cell 61, 274–286.
-
- Bianchi, A., Stansel, R.M., Fairall, L., Griffith, J.D., Rhodes, D., and de Lange, T. (1999). TRF1 binds a bipartite telomeric site with extreme spatial flexibility. EMBO J. 18, 5735–5744.
-
- Broccoli, D., Smogorzewska, A., Chong, L., and de Lange, T. (1997). Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat. Genet. 17, 231–235.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous