Restriction-modification (RM) systems are ubiquitous and are often considered primitive
immune systems in bacteria. Their diversity and prevalence across the prokaryotic kingdom …

More than 3000 type II restriction endonucleases have been discovered. They recognize
short, usually palindromic, sequences of 4–8 bp and, in the presence of Mg2+, cleave the …

This article continues the series of Surveys and Summaries on restriction endonucleases
(REases) begun this year in Nucleic Acids Research. Here we discuss 'Type II'REases, the …

Human tyrosyl-DNA phosphodiesterase (Tdp1) hydrolyzes the phosphodiester bond
between a DNA 3′ end and a tyrosyl moiety. In eukaryotic cells, this type of linkage is found …

DNA is subject to a wide range of insults, resulting from endogenous and exogenous
sources that need to be metabolized/resolved to maintain genome integrity. Tyrosyl-DNA …

Abstract Tyrosyl-DNA phosphodiesterase (Tdp1) is a member of the phospholipase D
superfamily and acts as a DNA repair enzyme that removes stalled topoisomerase I-DNA …

Tyrosyl-DNA phosphodiesterase (Tdp1) is a DNA repair enzyme that catalyzes the
hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3′-phosphate …

For a very long time, Type II restriction enzymes (REases) have been a paradigm of
ORFans: proteins with no detectable similarity to each other and to any other protein in the …

Type IIs restriction endonucleases recognize asymmetric DNA sequences and cleave both
DNA strands at fixed positions, typically several base pairs away from the recognition site …

The restriction enzyme R. BbvCI cleaves duplex DNA within a seven base-pair asymmetric
recognition sequence, thus: CCTCAGC/GCTGAGG→ CC^ TCAGC/GC^ TGAGG. We show …