Colicin E2 is DNA endonuclease.
نویسندگان
چکیده
منابع مشابه
Amount of Colicin Release in Escherichia coli Is Regulated by Lysis Gene Expression of the Colicin E2 Operon
The production of bacteriocins in response to worsening environmental conditions is one means of bacteria to outcompete other microorganisms. Colicins, one class of bacteriocins in Escherichia coli, are effective against closely related Enterobacteriaceae. Current research focuses on production, release and uptake of these toxins by bacteria. However, little is known about the quantitative aspe...
متن کاملThe zinc ion in the HNH motif of the endonuclease domain of colicin E7 is not required for DNA binding but is essential for DNA hydrolysis.
The HNH motif was originally identified in the subfamily of HNH homing endonucleases, which initiate the process of the insertion of mobile genetic elements into specific sites. Several bacteria toxins, including colicin E7 (ColE7), also contain the 30 amino acid HNH motif in their nuclease domains. In this work, we found that the nuclease domain of ColE7 (nuclease-ColE7) purified from Escheric...
متن کاملRelease of immunity protein requires functional endonuclease colicin import machinery.
Bacteria producing endonuclease colicins are protected against the cytotoxic activity by a small immunity protein that binds with high affinity and specificity to inactivate the endonuclease. This complex is released into the extracellular medium, and the immunity protein is jettisoned upon binding of the complex to susceptible cells. However, it is not known how and at what stage during infect...
متن کاملInhibition of colicin e2 activity by bacterial lipopolysaccharide.
Lipopolysaccharide isolated from colicin E2-sensitive Escherichia coli and from "receptor-minus" mutants inhibits the activity of colicin E2. Lipid A and the polysaccharide fraction obtained by mild acid hydrolysis of lipopolysaccharide are inactive either alone or when tested in combination. Periodate oxidation of lipopolysaccharide destroys over 85% of its inhibition activity.
متن کاملStabilization of colicin E2 by bovine serum albumin.
Colicin E2 was partially purified from Escherichia coli W3110. This preparation was remarkably stabilized by bovine serum albumin in a solution at neutral pH, as shown by dilution experiments and tests on heat stability of colicin. One killing unit of colicin E2 was estimated to correspond to one molecule of colicin E2, on the assumption of a molecular weight of 60,000.
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1976
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.73.11.3989