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Structural basis for protein-RNA recognition in telomerase.

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.

SUBMITTER: Huang J

PROVIDER: S-EPMC4409868 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Structural basis for protein-RNA recognition in telomerase.

Huang Jing J Brown Andrew F AF Wu Jian J Xue Jing J Bley Christopher J CJ Rand Dustin P DP Wu Lijie L Zhang Rongguang R Chen Julian J-L JJ Lei Ming M

Nature structural & molecular biology 20140504 6

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 ...[more]

PMID: 24793650

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