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1.
Fig 2

Fig 2. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

His4C expression and Suc2 glycosylation assays of Fks1 N-terminal and central domain fusions. His4C expression was assayed by comparing growth on SD-ura and SDh-ura-his media. N-linked glycosylation was assayed by Western blot detection of HA-tagged fusions either treated (+) or untreated (−) with Endo H; band shift indicates glycosylation. Fusions localized to the cytosol are underlined.

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.
2.
Fig 3

Fig 3. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

(A) His4C expression of Fks1 central and C-terminal domain fusions initiated at amino acid 1; (B) His4C expression and Suc2 glycosylation assays of Fks1 central and C-terminal domain fusions initiated at amino acid 1204. See the legend to Fig. 2 for details. Ambiguous results (lack of band shift but weak growth on SDh-ura-his) are indicated with a dashed underline.

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.
3.
Fig 6

Fig 6. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

Model of S. cerevisiae Fks1 membrane topology (red bars, TMH) and correlation with echinocandin resistance hot spots (yellow bars). Drawing is not to scale and does not attempt to show how the three hot spots might come together to form a single echinocandin binding pocket. Numbers represent Fks1 residue locations of C-terminal HA-Suc2-His4C fusions tested in this study (fusion 1410 omitted due to space constraints).

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.
4.
Fig 1

Fig 1. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

TMHMM-predicted TMH locations (residue number) and probabilities (P) for Fks1 from S. cerevisiae (Sc), C. albicans (Ca), A. fumigatus (Af), C. neoformans (Cn), R. oryzae (Ro), and A. macrogynus (Am). The PRO-TMHMM prediction was generated using S. cerevisiae Fks1 as a query. TMH on the same line are considered to be equivalent based on overlap in the Fks1 ClustalW2 alignment (see Fig. S1 in the supplemental material). np, not predicted; tr, truncated C terminus.

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.
5.
Fig 5

Fig 5. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

In silico and mutational analyses of Fks1 central domain. (A) Representative example of HHpred output using the S. cerevisiae Fks1 central domain as a query, showing apparent homology to a structurally defined bacterial glycosyltransferase. The DXD motif which coordinates Mn2+ interaction with UDP-glucose is underlined. (B) Alignment of Fks1 central domain regions from S. cerevisiae (Sc), the oomycete Phytophthora infestans (Pi), the plant Arabidopsis thaliana (At), and the protozoan Toxoplasma gondii (Tg). Sequences corresponding to the Neurospora crassa Fks1 peptides cross-linked to azido-UDP-glucose are overlined. Glycosyltransferase homology region within ScFks1 is in italics; residues that align with the DXD motif are underlined. (C) Functional analysis of Fks1 mutants D1102A and D1197A; see the legend to Fig. 4B for details. (D) ClustalW2 alignment of putative Fks1 catalytic regions equivalent to S. cerevisiae residues 1177 to 1221 from divergent species representing fungi, plants, and protists. Mutated S. cerevisiae residue D1197 is underlined.

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.
6.
Fig 4

Fig 4. From: Topological and Mutational Analysis of Saccharomyces cerevisiae Fks1.

Mutational analysis of a conserved residue within the Fks1 cytosolic N-terminal domain and truncation analysis of the external C terminus. (A) ClustalW2 alignment of S. cerevisiae Fks1 residues 300 to 335 and homologous sequences from divergent species: ascomycetes S. cerevisiae, C. albicans, and A. fumigatus; basidiomycete C. neoformans; zygomycete R. oryzae; plant Arabidopsis thaliana; oomycete Phytophthora infestans; diatom Phaeodactylum tricornutum; green alga Chlamydomonas reinhardtii; and apicomplexan Toxoplasma gondii. Asterisk, conserved in all sequences; colon, highly conservative substitution; period, less conservative substitution. (B) Functional analysis of plasmid-expressed wild-type (WT) versus R319A-mutated Fks1. Function was tested by comparing growth in an fks1::KANMX strain background with and without calcineurin inhibitor FK506 (1 μg/ml), which blocks FKS2 expression. (C) Functional analysis of full-length versus C-terminally truncated Fks1; see description of panel B for details.

Michael E. Johnson, et al. Eukaryot Cell. 2012 July;11(7):952-960.

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