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Fig. 1 | Epigenetics & Chromatin

Fig. 1

From: RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5

Fig. 1

Identification of Hsp90 and Mas5 as silencing factors. a Cells were serially diluted, spotted on normal YES plates (YES) and YES containing limited amount of adenine (low adenine) or 0.1% 5-FOA (5-FOA), and incubated at the indicated temperature for 3 days. Marker integration sites are shown in Additional file 1: Figure S4. b Results of sequencing of the antisense strand of the hsp90 gene. Arrows indicate the position of the base substitution. The wild-type cytosine at position 97 (with respect to the ORF start), which is guanine in the antisense strand, was replaced with thymine (adenine in the antisense strand) in the mutant. c Domain structure of Hsp90 family proteins. The N-terminal ATPase domains (ATPase), middle domains (M), and C-terminal domains (CT) are indicated. The names of proteins are associated with two-letter abbreviations indicating the species: “sp” for Schizosaccharomyces pombe (UniProt id: P41887), “sc” for Saccharomyces cerevisiae (P02829), “hs” for Homo sapience (P07900), and “ec” for Escherichia coli (P0A6Z3). The amino acid length (a.a.) of the proteins is shown. The position of R33C substitution is indicated with an asterisk. d Alignment of protein sequences around the R33C mutation. Residue numbers for the first and last amino acid residues for each protein interval are shown. Identical and similar residues are indicated as asterisks and colons, respectively, as seen in a standard ClustalW output. The residues corresponding to the Arg-33 in the fission yeast Hsp90 are colored in blue. The catalytic glutamate residues corresponding to the Glu-33 in budding yeast Hsp82 are colored in red

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