Cargando…

A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes

Restriction Modification (RM) systems prevent the invasion of foreign genetic material into bacterial cells by restriction and protect the host's genetic material by methylation. They are therefore important in maintaining the integrity of the host genome. RM systems are currently classified in...

Descripción completa

Detalles Bibliográficos
Autores principales: Bower, Edward K M, Cooper, Laurie P, Roberts, Gareth A, White, John H, Luyten, Yvette, Morgan, Richard D, Dryden, David T F
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158711/
https://www.ncbi.nlm.nih.gov/pubmed/30165537
http://dx.doi.org/10.1093/nar/gky760
_version_ 1783358470838288384
author Bower, Edward K M
Cooper, Laurie P
Roberts, Gareth A
White, John H
Luyten, Yvette
Morgan, Richard D
Dryden, David T F
author_facet Bower, Edward K M
Cooper, Laurie P
Roberts, Gareth A
White, John H
Luyten, Yvette
Morgan, Richard D
Dryden, David T F
author_sort Bower, Edward K M
collection PubMed
description Restriction Modification (RM) systems prevent the invasion of foreign genetic material into bacterial cells by restriction and protect the host's genetic material by methylation. They are therefore important in maintaining the integrity of the host genome. RM systems are currently classified into four types (I to IV) on the basis of differences in composition, target recognition, cofactors and the manner in which they cleave DNA. Comparing the structures of the different types, similarities can be observed suggesting an evolutionary link between these different types. This work describes the ‘deconstruction’ of a large Type I RM enzyme into forms structurally similar to smaller Type II RM enzymes in an effort to elucidate the pathway taken by Nature to form these different RM enzymes. Based upon the ability to engineer new enzymes from the Type I ‘scaffold’, an evolutionary pathway and the evolutionary pressures required to move along the pathway from Type I RM systems to Type II RM systems are proposed. Experiments to test the evolutionary model are discussed.
format Online
Article
Text
id pubmed-6158711
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Oxford University Press
record_format MEDLINE/PubMed
spelling pubmed-61587112018-10-02 A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes Bower, Edward K M Cooper, Laurie P Roberts, Gareth A White, John H Luyten, Yvette Morgan, Richard D Dryden, David T F Nucleic Acids Res Nucleic Acid Enzymes Restriction Modification (RM) systems prevent the invasion of foreign genetic material into bacterial cells by restriction and protect the host's genetic material by methylation. They are therefore important in maintaining the integrity of the host genome. RM systems are currently classified into four types (I to IV) on the basis of differences in composition, target recognition, cofactors and the manner in which they cleave DNA. Comparing the structures of the different types, similarities can be observed suggesting an evolutionary link between these different types. This work describes the ‘deconstruction’ of a large Type I RM enzyme into forms structurally similar to smaller Type II RM enzymes in an effort to elucidate the pathway taken by Nature to form these different RM enzymes. Based upon the ability to engineer new enzymes from the Type I ‘scaffold’, an evolutionary pathway and the evolutionary pressures required to move along the pathway from Type I RM systems to Type II RM systems are proposed. Experiments to test the evolutionary model are discussed. Oxford University Press 2018-09-28 2018-08-28 /pmc/articles/PMC6158711/ /pubmed/30165537 http://dx.doi.org/10.1093/nar/gky760 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Nucleic Acid Enzymes
Bower, Edward K M
Cooper, Laurie P
Roberts, Gareth A
White, John H
Luyten, Yvette
Morgan, Richard D
Dryden, David T F
A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title_full A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title_fullStr A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title_full_unstemmed A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title_short A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
title_sort model for the evolution of prokaryotic dna restriction-modification systems based upon the structural malleability of type i restriction-modification enzymes
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158711/
https://www.ncbi.nlm.nih.gov/pubmed/30165537
http://dx.doi.org/10.1093/nar/gky760
work_keys_str_mv AT boweredwardkm amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT cooperlauriep amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT robertsgaretha amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT whitejohnh amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT luytenyvette amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT morganrichardd amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT drydendavidtf amodelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT boweredwardkm modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT cooperlauriep modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT robertsgaretha modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT whitejohnh modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT luytenyvette modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT morganrichardd modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes
AT drydendavidtf modelfortheevolutionofprokaryoticdnarestrictionmodificationsystemsbaseduponthestructuralmalleabilityoftypeirestrictionmodificationenzymes