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. 2014 Aug 20;42(16):10711–10719. doi: 10.1093/nar/gku768

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© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Differential influence of amino acids at position -1 on efficiency of PPP-stalling. (A,B) Relative β-galactosidase activities of (A) NlpD-XPPP and (B) CadC-XPPP fusions with LacZ, where X represents one of the 20 proteinogenic amino acids, were determined by monitoring the β-galactosidase activities of the LacZ fusions in wild-type E. coli strains relative to the Δefp strain. Values were normalized relative to a control LacZ construct lacking the PPP motif (no stalling) which was assigned as 100%. (C) Scatter plot of relative β-galactosidase activities of NlpD-XPPP-LacZ relative to CadC-XPPP-LacZ constructs. (D) Scatter plot of relative β-galactosidase activities of CadC-XPPP-LacZ relative to CadC-XPP-LacZ fusions (8). (E) Chemical structure of proline in trans and cis conformation. (F) Possible trans and cis conformations of peptide containing aromatic amino acids followed by proline.