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Literature summary for 3.1.21.3 extracted from

  • Ohno, S.; Handa, N.; Watanabe-Matsui, M.; Takahashi, N.; Kobayashi, I.
    Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity (2008), J. Bacteriol., 190, 2039-2049.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strains BNH670 or GM31 harboring a plasmid with various versions of the EcoRII RM gene complex Escherichia coli

Protein Variants

Protein Variants Comment Organism
L80P L80P mutation in the modification enzyme of the EcoRII gene complex confers thermosensitivity of cell growth (shows activity at 30°C but not at 37°C). Under a condition of inhibited protein synthesis, the activity of the mutant is completely lost at a high temperature. In parallel, the L80P mutant protein disappears more rapidly than the wild-type protein Escherichia coli
additional information N-terminal 83-amino-acid deletion mutant, shows activity at at 30°C and 37°C. The EcoRII RM gene complex is a mutant carrying a T239C (L80P) substitution in the modification gene and a synonymous T402C substitution in the restriction gene. The capability of the restriction-modification system EcoRII in forcing maintenance on its host can be modulated by a region of its antitoxin, the modification enzyme, as in the classical postsegregational killing systems Escherichia coli
T239C shows decreased DNA methyltransferase activity at a higher temperature in vivo and in vitro than the nonmutated enzyme Escherichia coli
T402C cells carrying the mutation are able to grow at 42°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
EcoRII modification enzyme
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Escherichia coli
EcoRII RM gene complex
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Escherichia coli
EcoRII system
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Escherichia coli