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Figure 5


Fig. 5. Hydrophobic residues of the Ist2 sorting signal function as an amphipathic {alpha}-helix. (A) Presentation of residues K936-L946 as helical wheel projection. Hydrophobic leucines are marked in yellow, basic residues in blue, glycine in green and inserted alanines in grey. Depicted are wild-type Ist2, a mutant with an insertion of three alanines after position L938 and a mutant with insertion of four alanines after position G937. (B) Ist2 mutants with an exchange in the order of the leucine residues resulting in LxxLL and with an insertion of one or two alanines after position K941. The expression of the constructs in A and B was induced in sec23-1 cells for 120 minutes with galactose at 25°C or 37°C. (C,D) Secondary structure determination of the Ist2 933-946 peptide (C) and Ist2 L939P 933-946 peptide (D) by CD in 5 mM potassium phosphate buffer or in 20%, 40% and 50% TFE buffered with 5 mM potassium phosphate, respectively. The given spectra are the means of five measurements.





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