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  Restriction endonucleases that resemble a component of the bacterial DNA repair machinery

Sokolowska, M., Kaus-Drobek, M., Czapinska, H., Tamulaitis, G., Siksnys, V., & Bochtler, M. (2007). Restriction endonucleases that resemble a component of the bacterial DNA repair machinery. Cellular and Molecular Life Sciences, 64(18), 2351-2357.

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Sokolowska, M, Author
Kaus-Drobek, M, Author
Czapinska, H, Author
Tamulaitis, G, Author
Siksnys, V, Author
Bochtler, M1, Author           
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1Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 Abstract: It has long been known that most Type II restriction endonucleases share a conserved core fold and similar active-sites. The same core folding motif is also present in the MutH protein, a component of the bacterial DNA mismatch repair machinery. In contrast to most Type II restriction endonucleases, which assemble into functional dimers and catalyze double-strand breaks, MutH is a monomer and nicks hemimethylated DNA. Recent biochemical and crystallographic studies demonstrate that the restriction enzymes BcnI and MvaI share many additional features with MutH-like proteins, but not with most other restriction endonucleases. The structurally similar monomers all recognize approximately symmetric target sequences asymmetrically. Differential sensitivities to slight substrate asymmetries, which could be altered by protein engineering, determine whether the enzymes catalyze only single-strand nicks or double-strand breaks.

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 Dates: 2007
 Publication Status: Issued
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 Identifiers: eDoc: 348554
Other: 879
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Title: Cellular and Molecular Life Sciences
Source Genre: Journal
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Pages: - Volume / Issue: 64 (18) Sequence Number: - Start / End Page: 2351 - 2357 Identifier: -