Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 6, Pages 507-512Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2819
Keywords
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Funding
- Ministry of Science and Technology of China [2013CB910400]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08010201]
- US National Institutes of Health [RO1GM094450]
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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.
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