A mesophilic cysteine-less split intein for protein trans-splicing applications under oxidizing conditions.

ABSTRACT: Split intein-mediated protein trans-splicing has found extensive applications in chemical biology, protein chemistry, and biotechnology. However, an enduring limitation of all well-established split inteins has been the requirement to carry out the reaction in a reducing environment due to the presence of 1 or 2 catalytic cysteines that need to be in a reduced state for splicing to occur. The concomitant exposure of the fused proteins to reducing agents severely limits the scope of protein trans-splicing by excluding proteins sensitive to reducing conditions, such as those containing critical disulfide bonds. Here we report the discovery, characterization, and engineering of a completely cysteine-less split intein (CL intein) that is capable of efficient trans-splicing

SUBMITTER: Bhagawati M 

PROVIDER: S-EPMC6825276 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature