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

Authors: 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

Abstract

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.

Related Organizations
Keywords

DNA, Bacterial, Models, Molecular, Protein Conformation, alpha-Helical, 570, functional-analysis, modification enhancement, Protein Engineering, endonuclease, Evolution, Molecular, Structure-Activity Relationship, Escherichia coli, Protein Interaction Domains and Motifs, subunit, cleavage, Amino Acid Sequence, Deoxyribonucleases, Type II Site-Specific, Methyltransferase, Binding Sites, Models, Genetic, Nucleic Acid Enzymes, horizontal gene-transfer, Escherichia coli Proteins, Deoxyribonucleases, Type I Site-Specific, crystal-structure, sequence recognition, Protein Structure, Tertiary, Kinetics, Structural Homology, Protein, Protein Conformation, beta-Strand, protein, Protein Binding

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    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    16
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 10%
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Top 10%
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
16
Top 10%
Average
Top 10%
Green
gold