Structural Domains in the Type III Restriction Endonuclease EcoP15I: Characterization by Limited Proteolysis, Mass Spectrometry and Insertional Mutagenesis-Reference-Cited by-同舟云学术

Structural Domains in the Type III Restriction Endonuclease EcoP15I: Characterization by Limited Proteolysis, Mass Spectrometry and Insertional Mutagenesis

Published:2007-02 Issue:1 Volume:366 Page:93-102
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Wagenführ Katja,Pieper Stefan,Mackeldanz Petra,Linscheid Michael,Krüger Detlev H.,Reuter Monika

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference23 articles.

1. Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage;Meisel;Nature,1992

2. Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I;Janscak;J. Mol. Biol.,2001

3. Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis;Meisel;EMBO J.,1995

4. Functional cooperation between exonucleases and endonucleases–basis for the evolution of restriction enzymes;Raghavendra;Nucl. Acids Res.,2003

5. DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites;Mucke;J. Mol. Biol.,2001

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1. Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain;Biochimie;2013-04

2. DeepSuperSAGE: High-Throughput Transcriptome Sequencing with Now- and Next-Generation Sequencing Technologies;Tag-Based Next Generation Sequencing;2012-01-23

3. Mechanistic insights into type III restriction enzymes;Frontiers in Bioscience;2012

4. Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity;Nucleic Acids Research;2011-12-23

5. Diversity in Functional Organization of Class I and Class II Biotin Protein Ligase;PLoS ONE;2011-03-03