A report, "Generation of DNA cleavage specificities of type II restriction endonucleases by reassortment of target recognition domains," is newly published data in Proceedings of the National Academy of Sciences of the United States of America. According to recent research from Vilnius, Lithuania, "Type II restriction endonucleases (REases) cleave double-stranded DNA at specific sites within or close to their recognition sequences. Shortly after their discovery in 1970, REases have become one of the primary tools in molecular biology."

"However, the list of available specificities of type II REases is relatively short despite the extensive search for them in natural sources and multiple attempts to artificially change their specificity. In this study, we examined the possibility of generating cleavage specificities of REases by swapping putative target recognition domains (TRDs) between the type IIB enzymes AloI, PpiI, and TstI. Our results demonstrate that individual TRDs recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Based on these properties, we engineered a functional type IIB REase having previously undescribed DNA specificity," wrote S. Jurenaite-Urbanaviciene and colleagues, Institute of Biotechnology.

Read more on the report here.

Institute of Biotechnology, Vilnius, Lithuania