Figure 2. Ylr072w/Ltc1 is a member of a conserved protein family and catalyzes sterol transport between membranes. (A) Ltc1 family members in budding yeast and humans, also identified by Khafif et al. (2014). Members were identified by BLAST searches with the amino acid sequence of Ylr072w/Ltc1. Proteins with significant sequence similarity were queried for shared predicted secondary structure and domains with Phyre2 and i-TASSER (Kelley and Sternberg, 2009; Yang et al., 2015). In yeast, the paralogues Ltc1/Ltc2(Yfl042c) and Ltc3(Yhr080c)/Ltc4(Ysp2) arose from a genome duplication event. (B–D) Ltc1 selectively transports sterol between membranes (B; n = 4 for cholesterol and n = 2 for triolein and phospholipids) in a concentration (C; n = 4)- and time (D; with protein n = 3; control without protein n = 1)-dependent manner and were performed as depicted in the schematic in B and as described in Materials and methods. Errors bars represent standard deviation.
Figure 2.

Ylr072w/Ltc1 is a member of a conserved protein family and catalyzes sterol transport between membranes. (A) Ltc1 family members in budding yeast and humans, also identified by Khafif et al. (2014). Members were identified by BLAST searches with the amino acid sequence of Ylr072w/Ltc1. Proteins with significant sequence similarity were queried for shared predicted secondary structure and domains with Phyre2 and i-TASSER (Kelley and Sternberg, 2009; Yang et al., 2015). In yeast, the paralogues Ltc1/Ltc2(Yfl042c) and Ltc3(Yhr080c)/Ltc4(Ysp2) arose from a genome duplication event. (B–D) Ltc1 selectively transports sterol between membranes (B; n = 4 for cholesterol and n = 2 for triolein and phospholipids) in a concentration (C; n = 4)- and time (D; with protein n = 3; control without protein n = 1)-dependent manner and were performed as depicted in the schematic in B and as described in Materials and methods. Errors bars represent standard deviation.

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