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Title: Structure of the RNA-Binding Domain of Telomerase: Implications For RNA Recognition and Binding

Abstract

Telomerase, a ribonucleoprotein complex, replicates the linear ends of eukaryotic chromosomes, thus taking care of the 'end of replication problem.' TERT contains an essential and universally conserved domain (TRBD) that makes extensive contacts with the RNA (TER) component of the holoenzyme, and this interaction is thought to facilitate TERT/TER assembly and repeat-addition processivity. Here, we present a high-resolution structure of TRBD from Tetrahymena thermophila. The nearly all-helical structure comprises a nucleic acid-binding fold suitable for TER binding. An extended pocket on the surface of the protein, formed by two conserved motifs (CP and T motifs) comprises TRBD's RNA-binding pocket. The width and the chemical nature of this pocket suggest that it binds both single- and double-stranded RNA, possibly stem I, and the template boundary element (TBE). Moreover, the structure provides clues into the role of this domain in TERT/TER stabilization and telomerase repeat-addition processivity.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959986
Report Number(s):
BNL-82972-2009-JA
TRN: US201016%%1130
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 15; Journal Issue: 11
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CHROMOSOMES; RNA; STABILIZATION; TETRAHYMENA; national synchrotron light source

Citation Formats

Rouda,S., and Skordalakes, E. Structure of the RNA-Binding Domain of Telomerase: Implications For RNA Recognition and Binding. United States: N. p., 2007. Web. doi:10.1016/j.str.2007.09.007.
Rouda,S., & Skordalakes, E. Structure of the RNA-Binding Domain of Telomerase: Implications For RNA Recognition and Binding. United States. doi:10.1016/j.str.2007.09.007.
Rouda,S., and Skordalakes, E. Mon . "Structure of the RNA-Binding Domain of Telomerase: Implications For RNA Recognition and Binding". United States. doi:10.1016/j.str.2007.09.007.
@article{osti_959986,
title = {Structure of the RNA-Binding Domain of Telomerase: Implications For RNA Recognition and Binding},
author = {Rouda,S. and Skordalakes, E.},
abstractNote = {Telomerase, a ribonucleoprotein complex, replicates the linear ends of eukaryotic chromosomes, thus taking care of the 'end of replication problem.' TERT contains an essential and universally conserved domain (TRBD) that makes extensive contacts with the RNA (TER) component of the holoenzyme, and this interaction is thought to facilitate TERT/TER assembly and repeat-addition processivity. Here, we present a high-resolution structure of TRBD from Tetrahymena thermophila. The nearly all-helical structure comprises a nucleic acid-binding fold suitable for TER binding. An extended pocket on the surface of the protein, formed by two conserved motifs (CP and T motifs) comprises TRBD's RNA-binding pocket. The width and the chemical nature of this pocket suggest that it binds both single- and double-stranded RNA, possibly stem I, and the template boundary element (TBE). Moreover, the structure provides clues into the role of this domain in TERT/TER stabilization and telomerase repeat-addition processivity.},
doi = {10.1016/j.str.2007.09.007},
journal = {Structure},
number = 11,
volume = 15,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}