Abstract
Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.
Original language | English (US) |
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Pages (from-to) | 507-512 |
Number of pages | 6 |
Journal | Nature Structural and Molecular Biology |
Volume | 21 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2014 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
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Crystal structure of the TRBD domain of TERT and the CR4/5 of TR
Huang, J. (Contributor), Brown, A. F. (Contributor), Wu, J. (Contributor), Xue, J. (Contributor), Bley, C. J. (Contributor), Rand, D. P. (Contributor), Wu, L. (Contributor), Zhang, R. (Contributor), Chen, J. (Contributor) & Lei, M. (Contributor), Protein Data Bank (PDB), May 7 2014
DOI: 10.2210/pdb4O26, https://www.wwpdb.org/pdb?id=pdb_00004o26
Dataset