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Plos Biology : an Enzyme-catalyzed Multistep Dna Refolding Mechanism in Hairpin Telomere Formation, Volume 11

By Feigon, Juli

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Book Id: WPLBN0003922594
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos Biology : an Enzyme-catalyzed Multistep Dna Refolding Mechanism in Hairpin Telomere Formation, Volume 11  
Author: Feigon, Juli
Volume: Volume 11
Language: English
Subject: Journals, Science, Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Biology
Historic
Publication Date:
Publisher: Plos

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Feigon, J. (n.d.). Plos Biology : an Enzyme-catalyzed Multistep Dna Refolding Mechanism in Hairpin Telomere Formation, Volume 11. Retrieved from http://netlibrary.net/


Description
Description : Hairpin telomeres of bacterial linear chromosomes are generated by a DNA cutting–rejoining enzyme protelomerase. Protelomerase resolves a concatenated dimer of chromosomes as the last step of chromosome replication, converting a palindromic DNA sequence at the junctions between chromosomes into covalently closed hairpins. The mechanism by which protelomerase transforms a duplex DNA substrate into the hairpin telomeres remains largely unknown. We report here a series of crystal structures of the protelomerase TelA bound to DNA that represent distinct stages along the reaction pathway. The structures suggest that TelA converts a linear duplex substrate into hairpin turns via a transient strandrefolding intermediate that involves DNA-base flipping and wobble base-pairs. The extremely compact di-nucleotide hairpin structure of the product is fully stabilized by TelA prior to strand ligation, which drives the reaction to completion. The enzyme-catalyzed, multistep strand refolding is a novel mechanism in DNA rearrangement reactions.

 

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