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• W3092797611 endingPage "108250" @default.
• W3092797611 startingPage "108250" @default.
• W3092797611 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." @default.
• W3092797611 created "2020-10-22" @default.
• W3092797611 creator A5021524480 @default.
• W3092797611 creator A5056272083 @default.
• W3092797611 creator A5063572288 @default.
• W3092797611 creator A5071176976 @default.
• W3092797611 date "2020-10-01" @default.
• W3092797611 modified "2023-10-16" @default.
• W3092797611 title "Proteome-wide Capture of Co-translational Protein Dynamics in Bacillus subtilis Using TnDR, a Transposable Protein-Dynamics Reporter" @default.
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• W3092797611 doi "https://doi.org/10.1016/j.celrep.2020.108250" @default.

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