RNA conformation in catalytically active human telomerase.
We have used single-molecule fluorescence microscopy to study the folded state of human telomerase RNA (hTR). Here we show that hTR adopts a new conformation on binding to human telomerase reverse transcriptase (hTERT) and reconstitution of an active ribonucleoprotein complex. Our data are consistent with the formation of an RNA pseudoknot in active human telomerase.
Yeoman
Justin A
JA
The University Chemical Laboratory, University of Cambridge, UK.
Orte
Angel
A
Ashbridge
Beth
B
Klenerman
David
D
Balasubramanian
Shankar
S
D001483:Base Sequence; D055162:Biocatalysis; D004789:Enzyme Activation; D006801:Humans; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012313:RNA / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D019098:Telomerase / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
C422952:telomerase RNA; D012313:RNA; C509186:TERT protein, human; D019098:Telomerase