The structural biology of the shelterin complex

doi:10.1515/hsz-2018-0368

Review

. 2019 Mar 26;400(4):457-466.

doi: 10.1515/hsz-2018-0368.

The structural biology of the shelterin complex

Yong Chen^{1

2}

Affiliations

¹ State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 333 Haike Road, Shanghai 201210, China.
² School of Life Science and Technology, Shanghai Tech University, 100 Haike Road, Shanghai 201210, China.

PMID: 30352022
DOI: 10.1515/hsz-2018-0368

Free article

Review

The structural biology of the shelterin complex

Yong Chen. Biol Chem. 2019.

Free article

. 2019 Mar 26;400(4):457-466.

doi: 10.1515/hsz-2018-0368.

Author

Yong Chen^{1

2}

Affiliations

¹ State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, 333 Haike Road, Shanghai 201210, China.
² School of Life Science and Technology, Shanghai Tech University, 100 Haike Road, Shanghai 201210, China.

PMID: 30352022
DOI: 10.1515/hsz-2018-0368

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.

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References

1. Azad, G.K. and Tomar, R.S. (2016). The multifunctional transcription factor Rap1: a regulator of yeast physiology. Front Biosci. 21, 918–930.
1. Baumann, P. and Cech, T.R. (2001). Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171–1175.
1. 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.
1. 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.
1. 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.

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[1] Azad, G.K. and Tomar, R.S. (2016). The multifunctional transcription factor Rap1: a regulator of yeast physiology. Front Biosci. 21, 918–930.

[2] Azad, G.K. and Tomar, R.S. (2016). The multifunctional transcription factor Rap1: a regulator of yeast physiology. Front Biosci. 21, 918–930.

[3] Baumann, P. and Cech, T.R. (2001). Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171–1175.

[4] Baumann, P. and Cech, T.R. (2001). Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171–1175.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

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The structural biology of the shelterin complex

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