Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix

Clostridioides difficile adenine methyltransferase A (CamA) is required for the sporulation and colonization of the pathogen that causes gastrointestinal infections. Here, the authors characterise CamA kinetically and present its crystal structure bound to the DNA recognition sequence, which reveals...

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Main Authors: Jujun Zhou, John R. Horton, Robert M. Blumenthal, Xing Zhang, Xiaodong Cheng
Format: Article
Language:English
Published: Nature Publishing Group 2021-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23693-w
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spelling doaj-72d81f7c9e58495889a373df8da8fa712021-06-13T11:16:28ZengNature Publishing GroupNature Communications2041-17232021-06-0112111210.1038/s41467-021-23693-wClostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helixJujun Zhou0John R. Horton1Robert M. Blumenthal2Xing Zhang3Xiaodong Cheng4Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer CenterDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer CenterDepartment of Medical Microbiology and Immunology, and Program in Bioinformatics, The University of Toledo College of Medicine and Life SciencesDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer CenterDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer CenterClostridioides difficile adenine methyltransferase A (CamA) is required for the sporulation and colonization of the pathogen that causes gastrointestinal infections. Here, the authors characterise CamA kinetically and present its crystal structure bound to the DNA recognition sequence, which reveals DNA distortions including bending and the flipping of the target adenine out of the DNA helix, as well as protein conformational changes upon cofactor binding.https://doi.org/10.1038/s41467-021-23693-w
collection DOAJ
language English
format Article
sources DOAJ
author Jujun Zhou
John R. Horton
Robert M. Blumenthal
Xing Zhang
Xiaodong Cheng
spellingShingle Jujun Zhou
John R. Horton
Robert M. Blumenthal
Xing Zhang
Xiaodong Cheng
Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
Nature Communications
author_facet Jujun Zhou
John R. Horton
Robert M. Blumenthal
Xing Zhang
Xiaodong Cheng
author_sort Jujun Zhou
title Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
title_short Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
title_full Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
title_fullStr Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
title_full_unstemmed Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix
title_sort clostridioides difficile specific dna adenine methyltransferase cama squeezes and flips adenine out of dna helix
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-06-01
description Clostridioides difficile adenine methyltransferase A (CamA) is required for the sporulation and colonization of the pathogen that causes gastrointestinal infections. Here, the authors characterise CamA kinetically and present its crystal structure bound to the DNA recognition sequence, which reveals DNA distortions including bending and the flipping of the target adenine out of the DNA helix, as well as protein conformational changes upon cofactor binding.
url https://doi.org/10.1038/s41467-021-23693-w
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