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Updated: Dec 5, 2025

Real-Time Quantification of the Effects of IS200/IS605 Family-Associated TnpB on Transposon Activity
Published on: January 20, 2023
Proteome-wide Capture of Co-translational Protein Dynamics in Bacillus subtilis Using TnDR, a Transposable
Keigo Fujiwara1, Yutaro Katagi2, Koreaki Ito1
1Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku, Kyoto 603-8555, Japan; Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan.
Abstract:
Dynamic protein maturation, such as localization, folding, and complex formation, can occur co-translationally. To what extent do nascent polypeptides engage in the co-translational dynamics to produce the functional proteome's complement? We address this question using a protein-dynamics reporter (DR) module comprising a force-sensitive arrest sequence (Bacillus subtilis MifM) followed in frame by LacZ. An engineered transposon, TnDR, carrying DR, is transposed into the B. subtilis chromosome to create translational fusions between N-terminal regions of proteins and the C-terminal DR module. By looking for LacZ+ colonies, we identify hundreds of proteins that cancel the elongation arrest, most probably reflecting their ability to initiate the maturation/localization process co-translationally. Case studies identify B. subtilis proteins that initiate assembly with a partner molecule before completion of translation. These results suggest that co-translational maturation is a frequently occurring event in protein biogenesis.
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