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Science 30 March 2007: Vol. 315. no. 5820, pp. 1850 - 1853 DOI: 10.1126/science.1138596
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Reports
Protein Composition of Catalytically Active Human Telomerase from Immortal Cells
Scott B. Cohen,1
Mark E. Graham,2
George O. Lovrecz,3
Nicolai Bache,4
Phillip J. Robinson,2
Roger R. Reddel1*
Telomerase is a ribonucleoprotein enzyme complex that adds 5'-TTAGGG-3' repeats onto the ends of human chromosomes, providing a telomere maintenance mechanism for 90% of human cancers. We have purified human telomerase 108-fold, with the final elution dependent on the enzyme's ability to catalyze nucleotide addition onto a DNA oligonucleotide of telomeric sequence, thereby providing specificity for catalytically active telomerase. Mass spectrometric sequencing of the protein components and molecular size determination indicated an enzyme composition of two molecules each of telomerase reverse transcriptase, telomerase RNA, and dyskerin.
1 Cancer Research Unit, Children's Medical Research Institute, 214 Hawkesbury Road, Westmead NSW 2145, Australia.
2 Cell Signalling Unit, Children's Medical Research Institute, 214 Hawkesbury Road, Westmead NSW 2145, Australia.
3 Fermentation Lab, Commonwealth Scientific and Industrial Research Organisation, Molecular and Health Technologies, 343 Royal Parade, Parkville VIC 3052, Australia.
4 Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark.
* To whom correspondence should be addressed. E-mail: rreddel{at}cmri.usyd.edu.au
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