Ontology highlight
ABSTRACT:
SUBMITTER: Zylicz-Stachula A
PROVIDER: S-EPMC3384240 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Zylicz-Stachula Agnieszka A Zolnierkiewicz Olga O Lubys Arvydas A Ramanauskaite Danute D Mitkaite Goda G Bujnicki Janusz M JM Skowron Piotr M PM
BMC molecular biology 20120410
<h4>Background</h4>We previously defined a family of restriction endonucleases (REases) from Thermus sp., which share common biochemical and biophysical features, such as the fusion of both the nuclease and methyltransferase (MTase) activities in a single polypeptide, cleavage at a distance from the recognition site, large molecular size, modulation of activity by S-adenosylmethionine (SAM), and incomplete cleavage of the substrate DNA. Members include related thermophilic REases with five disti ...[more]