Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function

Title
Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function
Authors
김낙균Qi ZhangJuli Feigon
Issue Date
2014-03
Publisher
Nucleic acids research
Citation
VOL 42, NO 5, 3395-3408
Abstract
Telomerase is a unique reverse transcriptase that maintains the 30 ends of eukaryotic chromosomes by adding tandem telomeric repeats. The RNA subunit (TR) of vertebrate telomerase provides a template for reverse transcription, contained within the conserved template/pseudoknot domain, and a conserved regions 4 and 5 (CR4/5) domain, all essential for catalytic activity. We report the nuclear magnetic resonance (NMR) solution structure of the full-lengthCR4/ 5 domain from the teleost fish medaka (Oryzias latipes). Three helices emanate from a structured internal loop, forming a Y-shaped structure, where helix P6 stacks on P5 and helix P6.1 points away from P6. The relative orientations of the three helices are Mg2+ dependent and dynamic. Although the threeway junction is structured and has unexpected base pairs, telomerase activity assays with nucleotide substitutions and deletions in CR4/5 indicate that none of these are essential for activity. The results suggest that the junction is likely to change conformation in complex with telomerase reverse transcriptase and that it provides a flexible scaffold that allows P6 and P6.1 to correctly fold and interact with telomerase reverse transcriptase.
URI
http://pubs.kist.re.kr/handle/201004/48182
ISSN
03051048
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