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. 2006 Oct 23;175(2):249–259. doi: 10.1083/jcb.200605162

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Copyright © 2006, The Rockefeller University Press

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Figure 5. — The intermediate region of the int-atTic40 transit peptide is not required for membrane targeting. (A) [³⁵S]-labeled pre-atTic40 (FL) and deletion mutants spanning the indicated amino acids of pre-atTic40 were imported into isolated chloroplasts for 30 min and subsequently treated in the presence (+) or absence (−) of trypsin. IVT, 20% of the in vitro–translated protein used in each reaction. The graph presents quantitative analysis of the import efficiency of each construct presented as a percentage of the amount of import observed with wild-type pre-atTic40. (B) Analysis of total (T), soluble (S), and membrane (M) fractions of chloroplasts from 30-min import reactions of [³⁵S]-labeled pre-atTic40 and the transit peptide deletion mutants. The graph presents quantitative analysis of the distribution of the total atTic40 species between membrane and soluble fractions for each construct. (C) [³⁵S]pre-atTic40 and [³⁵S]pre-atTic40–Δ58-76 were imported into isolated pea chloroplasts for 5 min, treated with trypsin, reisolated, and incubated under import conditions for the times indicated. The total chloroplasts were separated into soluble and membrane fractions by alkaline extraction. Lanes 2 and 10 contain total (T) chloroplasts from the 5-min import reaction before protease treatment and subsequent incubation. Lanes 1 and 9 contain 20% of the translation product used for each of the import reactions.