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Nucleic Acids Research Advance Access originally published online on October 16, 2007
Nucleic Acids Research 2007 35(20):7011-7022; doi:10.1093/nar/gkm724
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Nucleic Acids Research, 2007, Vol. 35, No. 20 7011-7022
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Protein–RNA and protein–protein interactions mediate association of human EST1A/SMG6 with telomerase

Sophie Redon, Patrick Reichenbach and Joachim Lingner*

Swiss Institute for Experimental Cancer Research (ISREC), École Polytechnique Fédérale de Lausanne (EPFL) and National Center of Competence in Research ‘Frontiers in Genetics’, CH-1066 Epalinges s/Lausanne, Switzerland

*To whom correspondence should be addressed. Tel: +41 21 6925912; Fax: +41 21 6526933; Email: joachim.lingner{at}isrec.ch

Received July 4, 2007. Revised August 24, 2007. Accepted August 31, 2007.

The human EST1A/SMG6 polypeptide physically interacts with the chromosome end replication enzyme telomerase. In an attempt to better understand hEST1A function, we have started to dissect the molecular interactions between hEST1A and telomerase. Here, we demonstrate that the interaction between hEST1A and telomerase is mediated by protein–RNA and protein–protein contacts. We identify a domain within hEST1A that binds the telomerase RNA moiety hTR while full-length hEST1A establishes in addition RNase-resistant and hTR-independent protein–protein contacts with the human telomerase reverse transcriptase polypeptide (TERT). Conversely, within hTERT, we identify a hEST1A interaction domain, which comprises hTR-binding activity and RNA-independent hEST1A-binding activity. Purified, recombinant hEST1A binds the telomerase RNA moiety (hTR) with high affinity (apparent overall Kd = 25 nM) but low specificity. We propose that hEST1A assembles specifically with telomerase in the context of the hTR–hTERT ribonucleoprotein, through the high affinity of hEST1A for hTR and specific protein–protein contacts with hTERT.


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C. M. Azzalin, P. Reichenbach, L. Khoriauli, E. Giulotto, and J. Lingner
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[Abstract] [Full Text] [PDF]


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