Background: TET aminopeptidases are 12-subunit complexes present in the three domains of life and are involved in important biological functions. Results: The TET assembling process has been characterized. The oligomerization triggers TET activity toward large polypeptidic substrates. Conclusion:The assembling of TET is a controlled process and regulates its activity in vivo. Significance: This work provides a new example of peptidase regulation driven by self-oligomerization.

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The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododecameric TET peptidase machine, it was demonstrated that the assembly of the 12 subunits is a highly controlled process and represents a way to optimize the catalytic efficiency of the enzyme.