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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.
Cell Reports
|October 14, 2020
Summary
Nascent polypeptides frequently engage in co-translational dynamics, initiating protein maturation and localization before translation completion. This study reveals widespread co-translational events crucial for the functional proteome.
Area of Science:
- Molecular Biology
- Proteomics
- Cellular Biology
Background:
- Protein maturation, including folding and localization, can occur during translation.
- The extent to which nascent polypeptides participate in these co-translational dynamics is not fully understood.
Purpose of the Study:
- To investigate the prevalence of co-translational protein maturation and localization.
- To identify proteins that initiate these processes before completing translation.
Main Methods:
- Development of a protein-dynamics reporter (DR) module with a force-sensitive arrest sequence (MifM) fused to LacZ.
- Transposition of the engineered transposon (TnDR) into the *Bacillus subtilis* chromosome to create translational fusions.
- Identification of proteins that resolve translational arrest by screening for LacZ+ colonies.
Main Results:
- Hundreds of *Bacillus subtilis* proteins were identified that resolve translational arrest, suggesting co-translational maturation.
- Case studies demonstrated specific proteins initiating assembly with partners before translation termination.
- Co-translational maturation appears to be a common event in protein biogenesis.
Conclusions:
- Nascent polypeptides frequently engage in co-translational dynamics.
- This process is critical for producing the functional proteome.
- Co-translational maturation is a widespread phenomenon in protein biogenesis.
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