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.

journal_name

Nat Struct Mol Biol

authors

Huang J,Brown AF,Wu J,Xue J,Bley CJ,Rand DP,Wu L,Zhang R,Chen JJ,Lei M

doi

10.1038/nsmb.2819

subject

Has Abstract

pub_date

2014-06-01 00:00:00

pages

507-12

issue

6

eissn

1545-9993

issn

1545-9985

pii

nsmb.2819

journal_volume

21

pub_type

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