2MHI

Solution structure of the CR4/5 domain of medaka telomerase RNA

Summary for 2MHI

• Entry DOI: 10.2210/pdb2mhi/pdb
• NMR Information: BMRB: 19634
• Descriptor: Medaka telomerase RNA (1 entity in total)
• Functional Keywords: cr4-cr5, telomerase rna, three-way junction, vertebrate, medaka, rna
• Total number of polymer chains: 1
• Total formula weight: 16992.03

Authors

Kim, N.,Zhang, Q.,Feigon, J. (deposition date: 2013-11-23, release date: 2013-12-25, Last modification date: 2024-05-15)

Primary citation

Kim, N.K.,Zhang, Q.,Feigon, J.
Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function.
Nucleic Acids Res., 42:3395-3408, 2014

PubMed Abstract: Telomerase is a unique reverse transcriptase that maintains the 3' 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-length CR4/5 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 three-way 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.

PubMed: 24335084
DOI: 10.1093/nar/gkt1276

Experimental method

SOLUTION NMR