Split inteins arise from gene sequences embedded and separated within a host gene. Upon protein expression, individual intein fragments associate with each other and facilitate the intact host protein’s assembly in a process called protein splicing. Their efficient protein splicing ability makes inteins useful in protein engineering. In a study published article online on August 29 in the Journal of the American Chemical Society, David Cowburn, Ph.D., in collaboration with the laboratory of professor Tom Muir (Princeton University), describe a new group of atypically split inteins—split internally at an unusual location. To characterize atypical intein assembly and chemistry, they engineered a novel atypical intein with superior robustness and stability, called Cat, and demonstrated that this intein shows association mediated by hydrophobic interactions and distinct host sequence dependence properties. Cat is the fastest atypical split intein to date and should find immediate use in various technical applications. Dr. Cowburn is professor of biochemistry and of physiology and biophysics at Einstein.
Posted on: Monday, November 05, 2018