A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence

Bacteriophage repressor proteins downregulate viral lytic gene expression. Herein, the authors present the X-ray crystal structure of a monomeric repressor that binds an asymmetric DNA sequence using two independent domains.

Bibliographic Details
Published in:Nature Communications
Main Authors: Reliza J. McGinnis, Chad A. Brambley, Brandon Stamey, William C. Green, Kimberly N. Gragg, Erin R. Cafferty, Thomas C. Terwilliger, Michal Hammel, Thomas J. Hollis, Justin M. Miller, Maria D. Gainey, Jamie R. Wallen
Format: Article
Language:English
Published: Nature Portfolio 2022-07-01
Online Access:https://doi.org/10.1038/s41467-022-31678-6
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author Reliza J. McGinnis
Chad A. Brambley
Brandon Stamey
William C. Green
Kimberly N. Gragg
Erin R. Cafferty
Thomas C. Terwilliger
Michal Hammel
Thomas J. Hollis
Justin M. Miller
Maria D. Gainey
Jamie R. Wallen
author_facet Reliza J. McGinnis
Chad A. Brambley
Brandon Stamey
William C. Green
Kimberly N. Gragg
Erin R. Cafferty
Thomas C. Terwilliger
Michal Hammel
Thomas J. Hollis
Justin M. Miller
Maria D. Gainey
Jamie R. Wallen
author_sort Reliza J. McGinnis
collection DOAJ
container_title Nature Communications
description Bacteriophage repressor proteins downregulate viral lytic gene expression. Herein, the authors present the X-ray crystal structure of a monomeric repressor that binds an asymmetric DNA sequence using two independent domains.
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spelling doaj-art-c5e01eafbf234add839bb6caacf2cd402025-08-19T21:36:02ZengNature PortfolioNature Communications2041-17232022-07-0113111510.1038/s41467-022-31678-6A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequenceReliza J. McGinnis0Chad A. Brambley1Brandon Stamey2William C. Green3Kimberly N. Gragg4Erin R. Cafferty5Thomas C. Terwilliger6Michal Hammel7Thomas J. Hollis8Justin M. Miller9Maria D. Gainey10Jamie R. Wallen11Western Carolina University, Department of Chemistry and PhysicsMiddle Tennessee State University, Department of ChemistryWestern Carolina University, Department of Chemistry and PhysicsWestern Carolina University, Department of Chemistry and PhysicsWestern Carolina University, Department of Chemistry and PhysicsWestern Carolina University, Department of Chemistry and PhysicsNew Mexico ConsortiumMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National LaboratoryDepartment of Biochemistry, Wake Forest University School of Medicine, Medical Center BoulevardMiddle Tennessee State University, Department of ChemistryWestern Carolina University, Department of Chemistry and PhysicsWestern Carolina University, Department of Chemistry and PhysicsBacteriophage repressor proteins downregulate viral lytic gene expression. Herein, the authors present the X-ray crystal structure of a monomeric repressor that binds an asymmetric DNA sequence using two independent domains.https://doi.org/10.1038/s41467-022-31678-6
spellingShingle Reliza J. McGinnis
Chad A. Brambley
Brandon Stamey
William C. Green
Kimberly N. Gragg
Erin R. Cafferty
Thomas C. Terwilliger
Michal Hammel
Thomas J. Hollis
Justin M. Miller
Maria D. Gainey
Jamie R. Wallen
A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title_full A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title_fullStr A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title_full_unstemmed A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title_short A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence
title_sort monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric dna sequence
url https://doi.org/10.1038/s41467-022-31678-6
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