Phage N15 protelomerase resolves its tos recognition site into hairpin telomeres within mammalian cells

• Main Authors: Liew, Pei Sheng, Chen, Qingwen, Ng, Allan Wee Ren, Chew, Yee Choy, Ravin, Nikolai V., Sim, Edmund Ui Hang, Lee, Choon-Weng, Narayanan, Kumaran
• Format: E-Article
• Language: English
• Published: Elsevier Ltd. 2019
• Subjects: Q Science (General); QH426 Genetics
• Online Access: http://ir.unimas.my/id/eprint/25890/1/Phage%20N15%20protelomerase%20resolves%20its%20tos%20recognition%20site%20into%20hairpin%20-%20Copy.pdf; http://ir.unimas.my/id/eprint/25890/; https://www.sciencedirect.com/science/article/pii/S0003269719302209
• Institution: Universiti Malaysia Sarawak

Phage N15 protelomerase (TelN) cleaves double-stranded circular DNA containing a telomerase-occupancy-site (tos) and rejoins the resulting linear-ends to form closed-hairpin-telomeres in Escherichia coli (E. coli). ContinuedTelN expression is essential to support resolution of the linear structure....