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Structure of the motor subunit of type I restriction-modification complex EcoR124I


Lapkouski, M; Panjikar, S; Janscak, P; Smatanova, I K; Carey, J; Ettrich, R; Csefalvay, E (2009). Structure of the motor subunit of type I restriction-modification complex EcoR124I. Nature Structural and Molecular Biology, 16(1):94-95.

Abstract

Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.

Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2009
Deposited On:06 Feb 2010 14:15
Last Modified:05 Apr 2016 13:52
Publisher:Nature Publishing Group
ISSN:1545-9985
Publisher DOI:https://doi.org/10.1038/nsmb.1523
PubMed ID:19079266
Permanent URL: https://doi.org/10.5167/uzh-29704

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