Abstract
The Mrr protein of Escherichia coli K12 is a cryptic Type IV restriction endonuclease whose activity appears to be triggered by high pressure stress. In this report we used high pressure to isolate and analyze several Mrr mutants, and generated a new structural model of the Mrr protein. The activity of a number of spontaneous and strategically constructed Mrr mutants is discussed in the light of this model, providing a first insight into the structure-function relationships of the Mrr enzyme.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Amino Acid Sequence
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DNA Mutational Analysis
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DNA Restriction Enzymes / chemistry*
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DNA Restriction Enzymes / genetics*
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics*
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Models, Molecular*
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Molecular Sequence Data
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Pressure
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Protein Structure, Tertiary
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Structure-Activity Relationship
Substances
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Escherichia coli Proteins
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DNA Restriction Enzymes
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Mrr protein, E coli