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

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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Institution: Universiti Malaysia Sarawak
Language: English

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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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