Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1935240 | Biochemical and Biophysical Research Communications | 2008 | 5 Pages |
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.
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Authors
Jerzy Orlowski, Mehari Tesfazgi Mebrhatu, Chris W. Michiels, Janusz M. Bujnicki, Abram Aertsen,