Intein applications: from protein purification and labeling to metabolic control methods.
The discovery of inteins in the early 1990s opened the door to a wide variety of new technologies. Early engineered inteins from various sources allowed the development of self-cleaving affinity tags and new methods for joining protein segments through expressed protein ligation. Some applications were developed around native and engineered split inteins, which allow protein segments expressed separately to be spliced together in vitro. More recently, these early applications have been expanded and optimized through the discovery of highly efficient trans-splicing and trans-cleaving inteins. These new inteins have enabled a wide variety of applications in metabolic engineering, protein labeling, biomaterials construction, protein cyclization, and protein purification.
From the Department of Chemical and Biomolecular Engineering, Ohio State University, Columbus, Ohio 43210 and wood.750@osu.edu.
David W
DW
Wood
the Departments of Pharmacology and Pharmaceutical Sciences and Department of Chemistry, University of Southern California, Los Angeles, California 90033 jcamarer@usc.edu.
Julio A
JA
Camarero
D047668:Inteins / Q000235:genetics*; D015202:Protein Engineering / Q000379:methods / Q000639:trends; D019154:Protein Splicing / Q000235:genetics*; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013194:Staining and Labeling / Q000379:methods / Q000639:trends; D020040:Trans-Splicing / Q000235:genetics*
D011506:Proteins; D011993:Recombinant Fusion Proteins
Intein; Protein Chemical Modification; Protein Cyclization; Protein Engineering; Protein Labeling; Protein Processing; Protein Purification; Protein Self-assembly; Protein Splicing; Self-cleaving Tag