A functional interplay between intein and extein sequences in protein splicing compensates for the essential block B histidine.

ABSTRACT: Inteins remove themselves from a precursor protein by protein splicing. Due to the concomitant structural changes of the host protein, this self-processing reaction has enabled many applications in protein biotechnology and chemical biology. We show that the evolved M86 mutant of the Ssp DnaB intein displays a significantly improved tolerance towards non-native amino acids at the N-terminally flanking (-1) extein position compared to the parent intein, in the form of both an artificially trans-splicing split intein and the cis-splicing mini-intein. Surprisingly, side chains with increased steric bulk compared to the native Gly(-1) residue, including d-amino acids, were found to compensate for the essential block B histidine in His73Ala mutants in the initial N-S acyl s

SUBMITTER: Friedel K 

PROVIDER: S-EPMC6333167 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature