Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA

Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA

The cyanophage S-2L incorporates 2-aminoadenine (Z) instead of adenine into its DNA, which still pairs with thymine forming a triple hydrogen bond. Here, the authors identify a third gene mazZ located between purZ and datZ that is required for 2-aminoadenine biosynthesis and determine the crystal st...

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Main Authors: Dariusz Czernecki, Frédéric Bonhomme, Pierre-Alexandre Kaminski, Marc Delarue
Format: Article
Language:English
Published: Nature Publishing Group 2021-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-25064-x
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spelling doaj-2c5f8be15bf64c02b05de1d016baf9722021-08-08T11:37:00ZengNature Publishing GroupNature Communications2041-17232021-08-011211910.1038/s41467-021-25064-xCharacterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNADariusz Czernecki0Frédéric Bonhomme1Pierre-Alexandre Kaminski2Marc Delarue3Unit of Architecture and Dynamics of Biological Macromolecules, CNRS UMR 3528, 25-28 rue du Docteur Roux, Institut PasteurUnit of Epigenetic Chemical Biology, CNRS UMR 3523, 25-28 rue du Docteur Roux, Institut PasteurUnit of Biology of Pathogenic Gram-Positive Bacteria, CNRS UMR 2001, 25-28 rue du Docteur Roux, Institut PasteurUnit of Architecture and Dynamics of Biological Macromolecules, CNRS UMR 3528, 25-28 rue du Docteur Roux, Institut PasteurThe cyanophage S-2L incorporates 2-aminoadenine (Z) instead of adenine into its DNA, which still pairs with thymine forming a triple hydrogen bond. Here, the authors identify a third gene mazZ located between purZ and datZ that is required for 2-aminoadenine biosynthesis and determine the crystal structures of MazZ and PurZ. They further show that co-expression of these three genes in E.coli enables 2-aminoadenine incorporation into the bacterial genome.https://doi.org/10.1038/s41467-021-25064-x
collection DOAJ
language English
format Article
sources DOAJ
author Dariusz Czernecki
Frédéric Bonhomme
Pierre-Alexandre Kaminski
Marc Delarue
spellingShingle Dariusz Czernecki
Frédéric Bonhomme
Pierre-Alexandre Kaminski
Marc Delarue
Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
Nature Communications
author_facet Dariusz Czernecki
Frédéric Bonhomme
Pierre-Alexandre Kaminski
Marc Delarue
author_sort Dariusz Czernecki
title Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
title_short Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
title_full Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
title_fullStr Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
title_full_unstemmed Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA
title_sort characterization of a triad of genes in cyanophage s-2l sufficient to replace adenine by 2-aminoadenine in bacterial dna
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-08-01
description The cyanophage S-2L incorporates 2-aminoadenine (Z) instead of adenine into its DNA, which still pairs with thymine forming a triple hydrogen bond. Here, the authors identify a third gene mazZ located between purZ and datZ that is required for 2-aminoadenine biosynthesis and determine the crystal structures of MazZ and PurZ. They further show that co-expression of these three genes in E.coli enables 2-aminoadenine incorporation into the bacterial genome.
url https://doi.org/10.1038/s41467-021-25064-x
work_keys_str_mv AT dariuszczernecki characterizationofatriadofgenesincyanophages2lsufficienttoreplaceadenineby2aminoadenineinbacterialdna
AT fredericbonhomme characterizationofatriadofgenesincyanophages2lsufficienttoreplaceadenineby2aminoadenineinbacterialdna
AT pierrealexandrekaminski characterizationofatriadofgenesincyanophages2lsufficienttoreplaceadenineby2aminoadenineinbacterialdna
AT marcdelarue characterizationofatriadofgenesincyanophages2lsufficienttoreplaceadenineby2aminoadenineinbacterialdna
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