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Nucleic Acids Research, 2003, Vol. 31, No. 22 6509-6515
© 2003 Oxford University Press

Article

Identification of a new RNA·RNA interaction site for human telomerase RNA (hTR): structural implications for hTR accumulation and a dyskeratosis congenita point mutation

Xiaojun Ren, Gérald Gavory, Haitao Li, Liming Ying, David Klenerman and Shankar Balasubramanian*

Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK

*To whom correspondence should be addressed. Tel: +44 1223 336347; Fax: +44 1223 336913; Email sb10031{at}cam.ac.uk
Correspondence may also be addressed to David Klenerman. Tel: +44 1223 336481; Fax: +44 1223 336362; dk10012{at}cus.cam.ac.uk
The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors

The enzyme telomerase is a ribonucleoprotein that has a critical role in the maintenance of stable telomeres in organisms that possess linear chromosomes. Using a recently developed single molecule fluorescence coincidence method, we have studied the RNA component of telomerase (hTR) and directly observed multimerisation of hTR in solution. RNA mutagenesis and blocking oligonucleotides were employed to identify the single-stranded internal loop J7b/8a as an important and specific hTR·hTR interaction site. This observation was confirmed by studies on a model RNA fragment (hTR380–444), comprising part of the H/ACA domain, the internal loop J7b/8a and the CR7 domain, that was found to dimerise. Substitution mutagenesis within the proposed RNA·RNA interaction site of hTR380–444 resulted in a loss of dimerisation potential and insertion of the dyskeratosis congenita mutation C408G led to a significant reduction in dimer formation. Together, these results suggest that this RNA·RNA interaction site may be functionally relevant.


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