Structural basis for protein-RNA recognition in telomerase

Jing Huang, Andrew F. Brown, Jian Wu, Jing Xue, Christopher J. Bley, Dustin P. Rand, Lijie Wu, Rongguang Zhang, Julian Chen, Ming Lei

Research output: Contribution to journalArticlepeer-review

65 Scopus citations


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 languageEnglish (US)
Pages (from-to)507-512
Number of pages6
JournalNature Structural and Molecular Biology
Issue number6
StatePublished - Jun 2014

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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