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New PDF release: BioNMR in Drug Research

By O. Zerbe

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On the other hand, the split intein approach does not require any additional thionucleophile, in contrast to the IPL/EPL approach. Remarkably, this method can even be extended to joining three segments by using two different inteins, PI-PfuI and PI-PfuII (Fig. 5 C). Otomo et al. have successfully demonstrated this approach by isotope labeling a central segment of the 370-residue maltosebinding protein [71]. Three protein fragments were constructed for the two ligation reactions. The first fragment was a fusion protein of the N-terminal domain of the split target protein and the N-terminal split intein-1.

The potential to incorporate stable isotopes would facilitate structure determination by NMR techniques. Although NMR technologies were long considered to be applicable only to smaller proteins, the development of transverse relaxation-optimized spectroscopy (TROSY) has made it possible to use NMR for larger proteins also [5], even integral membrane proteins. For example, the OmpX and OmpA integral membrane proteins of E. coli were labeled with 13C/15N/2H isotopes and overexpressed as inclusion bodies in bacterial cells.

This trans-splicing activity can be directly used for protein ligation as an alternative to the native chemical ligation step, which requires additional thionucleophile groups. Yamazaki et al. have applied trans-splicing to the segmental labeling of RNA polymerase subunit a by splitting an intein from Pyrococcus furiosus, PI-PfuI (Fig. 5 B) [70]. Each half of the split intein fused to the N- (or C)-extein was produced separately, one in isotopically labeled and the other in unlabeled medium. The independently prepared protein fragments were expressed as inclusion bodies and purified under denaturing conditions.

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