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- W2085829147 abstract "POT1 (protection of telomeres 1) protein binds the G-rich single-stranded telomeric DNA at the ends of chromosomes. In human cells hPOT1 is involved in telomere length regulation, but the mechanism of this regulation remains unknown. Examination of the high-resolution crystal structure of the hPOT1-TTAGGGTTAG complex suggested that it would not be extended by telomerase, a hypothesis that we confirm by <i>in vitro</i> assays with recombinant telomerase. On the other hand, when hPOT1 is bound at a position one telomeric repeat before the 3′-end, leaving an 8-nucleotide 3′-tail, the complex is extended with improved activity and processivity. Thus, depending on its location relative to the DNA 3′-end, hPOT1 can either inhibit telomerase action or form a preferred substrate for telomerase. We propose that another factor catalyzes the interconversion of these states <i>in vivo</i>." @default.
- W2085829147 created "2016-06-24" @default.
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- W2085829147 date "2005-05-01" @default.
- W2085829147 modified "2023-10-13" @default.
- W2085829147 title "Switching Human Telomerase On and Off with hPOT1 Protein in Vitro" @default.
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- W2085829147 doi "https://doi.org/10.1074/jbc.m502212200" @default.
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