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. 2008 Jun 25;36(13):4233–4241. doi: 10.1093/nar/gkn395

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© 2008 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — The inhibition of protein synthesis from the reporter +7 AGA lacZ construct depends inversely on the length of the AGAAGAUAA minigenes. (A) In vitro transcription–translation reactions were directed by: +7 AGA lacZ (a); +7 placZ plus: placZ2-3AGAGAUAA (b); placZ3-4AGAAGAUAA (c); placZ4-5AGAAGAUAA (d); placZ5-6AGAAGAUAA (e); placZ6-7AGAAGAUAA (f); placZ7-8AGAAGAUAA (g). The mobility of β-galactosidase (β-gal) and β-lactamase (β-lac) is indicated. β-Gal absolute radioactivity levels are indicated as electronic density values (pixels, shown below each lane). (B) In vitro reactions were primed as in (A) but lacZ replaced +7 AGA lacZ. β-Gal synthesis from the reporter +7 AGA lacZ (C) or lacZ (D) constructs was plotted against minigene length.