BBa_K624053
BBa_K624053 Version 1 (Component)
mcherry+minC+RBS+tetO+pT7 + pT7+RBS+tetR+GFP

BBa_K624054
BBa_K624054 Version 1 (Component)
mcherry+minC+RBS+tetO+Pmsp1 + Pmsp1+RBS+tetR+GFP

BBa_K360141
BBa_K360141 Version 1 (Component)
Min. Blue Promoter + RBS + GFP BBa_E0040

BBa_K360044
BBa_K360044 Version 1 (Component)
Min. Blue Promoter BBa_K360041 + Mutated Red Luciferase BBa_K360115

BBa_K299806
BBa_K299806 Version 1 (Component)
minC cell division inhibitor

BBa_J29040
BBa_J29040 Version 1 (Component)
MinC

GFP-ASV
BBa_K1639023 Version 1 (Component)
GFP with an ASV degradation tag with a half-life of ~110 min

Intein_assisted_Bisection_Mapping
Intein_assisted_Bisection_Mapping_collection Version 1 (Collection)
Split inteins are powerful tools for seamless ligation of synthetic split proteins. Yet, their use remains limited because the already intricate split site identification problem is often complicated by the requirement of extein junction sequences. To address this, we augmented a mini-Mu transposon-based screening approach and devised the intein-assisted bisection mapping (IBM) method. IBM robustly revealed clusters of split sites on five proteins, converting them into AND or NAND logic gates. We further showed that the use of inteins expands functional sequence space for splitting a protein. We also demonstrated the utility of our approach over rational inference of split sites from secondary structure alignment of homologous proteins. Furthermore, the intein inserted at an identified site could be engineered by the transposon again to become partially chemically inducible, and to some extent enabled post-translational tuning on host protein function. Our work offers a generalizable and systematic route towards creating split protein-intein fusions and conditional inteins for protein activity control.