Skip to main content
Journal cover image

The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme.

Publication ,  Journal Article
Lattmann, S; Stadler, MB; Vaughn, JP; Akman, SA; Nagamine, Y
Published in: Nucleic Acids Res
November 2011

Guanine-quadruplexes (G4) consist of non-canonical four-stranded helical arrangements of guanine-rich nucleic acid sequences. The bulky and thermodynamically stable features of G4 structures have been shown in many respects to affect normal nucleic acid metabolism. In vivo conversion of G4 structures to single-stranded nucleic acid requires specialized proteins with G4 destabilizing/unwinding activity. RHAU is a human DEAH-box RNA helicase that exhibits G4-RNA binding and resolving activity. In this study, we employed RIP-chip analysis to identify en masse RNAs associated with RHAU in vivo. Approximately 100 RNAs were found to be associated with RHAU and bioinformatics analysis revealed that the majority contained potential G4-forming sequences. Among the most abundant RNAs selectively enriched with RHAU, we identified the human telomerase RNA template TERC as a true target of RHAU. Remarkably, binding of RHAU to TERC depended on the presence of a stable G4 structure in the 5'-region of TERC, both in vivo and in vitro. RHAU was further found to associate with the telomerase holoenzyme via the 5'-region of TERC. Collectively, these results provide the first evidence that intramolecular G4-RNAs serve as physiologically relevant targets for RHAU. Furthermore, our results suggest the existence of alternatively folded forms of TERC in the fully assembled telomerase holoenyzme.

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

November 2011

Volume

39

Issue

21

Start / End Page

9390 / 9404

Location

England

Related Subject Headings

  • Telomerase
  • Ribonucleoproteins
  • RNA-Binding Proteins
  • RNA
  • Oligonucleotide Array Sequence Analysis
  • Nucleotide Motifs
  • Humans
  • Holoenzymes
  • G-Quadruplexes
  • Developmental Biology
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Lattmann, S., Stadler, M. B., Vaughn, J. P., Akman, S. A., & Nagamine, Y. (2011). The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme. Nucleic Acids Res, 39(21), 9390–9404. https://doi.org/10.1093/nar/gkr630
Lattmann, Simon, Michael B. Stadler, James P. Vaughn, Steven A. Akman, and Yoshikuni Nagamine. “The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme.Nucleic Acids Res 39, no. 21 (November 2011): 9390–9404. https://doi.org/10.1093/nar/gkr630.
Lattmann S, Stadler MB, Vaughn JP, Akman SA, Nagamine Y. The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme. Nucleic Acids Res. 2011 Nov;39(21):9390–404.
Lattmann, Simon, et al. “The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme.Nucleic Acids Res, vol. 39, no. 21, Nov. 2011, pp. 9390–404. Pubmed, doi:10.1093/nar/gkr630.
Lattmann S, Stadler MB, Vaughn JP, Akman SA, Nagamine Y. The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in TERC and associates with telomerase holoenzyme. Nucleic Acids Res. 2011 Nov;39(21):9390–9404.
Journal cover image

Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

November 2011

Volume

39

Issue

21

Start / End Page

9390 / 9404

Location

England

Related Subject Headings

  • Telomerase
  • Ribonucleoproteins
  • RNA-Binding Proteins
  • RNA
  • Oligonucleotide Array Sequence Analysis
  • Nucleotide Motifs
  • Humans
  • Holoenzymes
  • G-Quadruplexes
  • Developmental Biology