title: The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats.
abstract: I have identified an activity in crude HeLa cell extracts that satisfies the requirements for a human telomere terminal transferase or telomerase. It catalyzes the addition of a 6 nucleotide repeating pattern to oligonucleotide primers containing human or nonhuman telomeric repeat sequences. Direct sequence analyses of reaction products reveal the added sequence to be TTAGGG in all cases. Under optimal conditions 65-70 repeats can be synthesized. The enzyme has the properties of a ribonucleoprotein. Telomerase has previously been observed only in ciliated protozoans, which possess 10(4) - 10(7) macronuclear telomeres. The identification of telomerase in HeLa cells with only approximately 100 telomeres indicates that telomerase-mediated telomere maintenance is conserved throughout eukaryotes.
authors: Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
authors: G B
authors: GB
authors: Morin
mesh_terms: D001483:Base Sequence; D002877:Chromosomes, Human / Q000201:enzymology; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000138:chemical synthesis; D012091:Repetitive Sequences, Nucleic Acid; D012261:Ribonucleoproteins / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D009838:Oligodeoxyribonucleotides; D012261:Ribonucleoproteins; D004254:DNA Nucleotidyltransferases; C056773:telomere terminal transferase