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Fig. 1. Hsp150 variants and dependence of their ER exit on functional Sec24p. (A) The product of the HSP150 gene has an N-terminal 18 amino acid signal peptide (SP, black). The ER form consists of a 54 amino acid subunit I (SU I, gray) and subunit II (SU II), which is composed of a repetitive region (RR) where homologous peptides of mostly 19 amino acids are repeated 11 times (diagonally striped boxes), followed by a unique C-terminal fragment (white area). (B) The last 89 amino acids of Hsp150 were deleted. (C) The C-terminal 114 amino acids of Hsp150 were joined to subunit I. (D) E. coli ß-lactamase (criss-crossed) was joined to subunit I. (E) HRP (checkered) was fused to the first 321 amino acids of Hsp150. (F) Invertase (horizontally striped) was fused to subunit I, and Cterm was fused to the C-terminus of invertase. (G) Invertase was fused to the C-terminus of SUI-Cterm. The last amino acids of the various domains are numbered. Letters indicate extra amino acids resulting from cloning strategy. All other proteins had a Kex2p recognition site at the C-terminal end of subunit I, except SUI-ß-lactamase (D) and Hsp150-HRP (E). The dependency of ER exit on functional Sec24p is indicated.

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