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.
The University Chemical Laboratory, University of Cambridge, UK.
Justin A
JA
Yeoman
Angel
A
Orte
Beth
B
Ashbridge
David
D
Klenerman
Shankar
S
Balasubramanian
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