Cargando…

The solution structure of an anti-CRISPR protein

Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems...

Descripción completa

Detalles Bibliográficos
Autores principales: Maxwell, Karen L., Garcia, Bianca, Bondy-Denomy, Joseph, Bona, Diane, Hidalgo-Reyes, Yurima, Davidson, Alan R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062604/
https://www.ncbi.nlm.nih.gov/pubmed/27725669
http://dx.doi.org/10.1038/ncomms13134
_version_ 1782459811431972864
author Maxwell, Karen L.
Garcia, Bianca
Bondy-Denomy, Joseph
Bona, Diane
Hidalgo-Reyes, Yurima
Davidson, Alan R.
author_facet Maxwell, Karen L.
Garcia, Bianca
Bondy-Denomy, Joseph
Bona, Diane
Hidalgo-Reyes, Yurima
Davidson, Alan R.
author_sort Maxwell, Karen L.
collection PubMed
description Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems using distinct mechanisms. Here, we present the three-dimensional structure of an anti-CRISPR protein and map a functional surface that is critical for its potent inhibitory activity. The interaction of the anti-CRISPR protein with the CRISPR–Cas complex through this functional surface is proposed to prevent the binding of target DNA.
format Online
Article
Text
id pubmed-5062604
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-50626042016-10-27 The solution structure of an anti-CRISPR protein Maxwell, Karen L. Garcia, Bianca Bondy-Denomy, Joseph Bona, Diane Hidalgo-Reyes, Yurima Davidson, Alan R. Nat Commun Article Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems using distinct mechanisms. Here, we present the three-dimensional structure of an anti-CRISPR protein and map a functional surface that is critical for its potent inhibitory activity. The interaction of the anti-CRISPR protein with the CRISPR–Cas complex through this functional surface is proposed to prevent the binding of target DNA. Nature Publishing Group 2016-10-11 /pmc/articles/PMC5062604/ /pubmed/27725669 http://dx.doi.org/10.1038/ncomms13134 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Maxwell, Karen L.
Garcia, Bianca
Bondy-Denomy, Joseph
Bona, Diane
Hidalgo-Reyes, Yurima
Davidson, Alan R.
The solution structure of an anti-CRISPR protein
title The solution structure of an anti-CRISPR protein
title_full The solution structure of an anti-CRISPR protein
title_fullStr The solution structure of an anti-CRISPR protein
title_full_unstemmed The solution structure of an anti-CRISPR protein
title_short The solution structure of an anti-CRISPR protein
title_sort solution structure of an anti-crispr protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062604/
https://www.ncbi.nlm.nih.gov/pubmed/27725669
http://dx.doi.org/10.1038/ncomms13134
work_keys_str_mv AT maxwellkarenl thesolutionstructureofananticrisprprotein
AT garciabianca thesolutionstructureofananticrisprprotein
AT bondydenomyjoseph thesolutionstructureofananticrisprprotein
AT bonadiane thesolutionstructureofananticrisprprotein
AT hidalgoreyesyurima thesolutionstructureofananticrisprprotein
AT davidsonalanr thesolutionstructureofananticrisprprotein
AT maxwellkarenl solutionstructureofananticrisprprotein
AT garciabianca solutionstructureofananticrisprprotein
AT bondydenomyjoseph solutionstructureofananticrisprprotein
AT bonadiane solutionstructureofananticrisprprotein
AT hidalgoreyesyurima solutionstructureofananticrisprprotein
AT davidsonalanr solutionstructureofananticrisprprotein