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

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....

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Bibliographic Details
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
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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

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