Proofreading of substrate structure by the Twin-Arginine Translocase is highly dependent on substrate conformational flexibility but surprisingly tolerant of surface charge and hydrophobicity changes
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- 作者：Alexander S. Jonesa ; James I. Austerberryb ; Rana Dajanib ; Jim Warwickerb ; Robin Curtisc ; Jeremy P. Derrickb ; Colin Robinsona ; c.robinson-504@kent.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：Tat ; Twin-Arginine Translocase ; Signal peptide ; Protein translocation
- 刊名：Biochimica et Biophysica Acta (BBA)-Molecular Cell Research
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：1863
- 期：12
- 页码：3116-3124
- 全文大小：1225 K
文摘
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The E. coli Tat system preferentially transports correctly folded proteins.
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We show that substantial charge/hydrophobicity changes to a substrate's surface are tolerated.
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Formation of intra-chain disulphide bonds is not required for folding but is essential for efficient translocation.
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Addition of a 26-residue disordered ‘tail’ blocks translocation.
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The data suggest that Tat measures the conformational flexibility of substrates.