NDLI: The monomeric homing endonuclease PI-SceI has two catalytic centres for cleavage of the two strands of its DNA substrate.

Content Provider	PubMed Central
Author	Christ, F. Schoettler, S. Wende, W. Steuer, S. Pingoud, A. Pingoud, V.
Abstract	The monomeric homing endonuclease PI-SceI cleaves the two strands of its DNA substrate in a concerted manner, which raises the question of whether this enzyme harbours one or two catalytic centres. If PI-SceI has only one catalytic centre, one would expect that cross-linking enzyme and substrate should prevent reorientation of the enzyme required to perform the second cut after having made the first cut: PI-SceI, however, when cross-linked to its substrate, is able to cleave both DNA strands. If PI-SceI has two catalytic centres, one would expect that it should be possible to inactivate one catalytic centre by mutation and obtain a variant with preference for a substrate nicked in one strand; such variants have been found. The structural homology between the catalytic domain of PI-SceI having a pseudo 2-fold symmetry, and I-CreI, a homodimeric homing endonuclease, suggests that in PI-SceI active site I, which attacks the top strand, comprises Asp218, Asp229 and Lys403, while Asp326, Thr341 and Lys301 make up active site II, which cleaves the bottom strand. Cleavage experiments with modified oligodeoxynucleotides and metal ion mapping experiments demonstrate that PI-SceI interacts differently with the two strands at the cleavage position, supporting a model of two catalytic centres.
Related Links	http://dx.doi.org/10.1093/emboj/18.24.6908
Ending Page	6916
Page Count	9
Starting Page	6908
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	24
Volume Number	18
Language	English
Publisher Date	1999-12-15
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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Binding, Bending and Cleavage of DNA Substrates by the Homing Endonuclease PI-SceI

A Mutational Analysis of DNA Binding and Cleavage by the Homing Endonuclease PI-SceI

Identification of Lys-403 in the PI-SceI Homing Endonuclease as Part of a Symmetric Catalytic Center

Substitutions in Conserved Dodecapeptide Motifs That Uncouple the DNA Binding and DNA Cleavage Activities of PI-SceI Endonuclease

The protein splicing domain of the homing endonuclease PI-SceI is responsible for specific DNA binding

Binding, bending and cleavage of DNA substrates by the homing endonuclease Pl-SceI.

DNA Recognition by the Homing Endonuclease PI-SceI Involves a Divalent Metal Ion Cofactor-induced Conformational Change

Conditional genomic rearrangement by designed meiotic recombination using VDE (PI-SceI) in yeast

The structure-specific endonuclease Mus81–Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks

The monomeric homing endonuclease PI-SceI has two catalytic centres for cleavage of the two strands of its DNA substrate.

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Binding, Bending and Cleavage of DNA Substrates by the Homing Endonuclease PI-SceI

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Identification of Lys-403 in the PI-SceI Homing Endonuclease as Part of a Symmetric Catalytic Center

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