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. 2013 Jun 15;24(12):2034–2044. doi: 10.1091/mbc.E12-12-0893

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© 2013 Boeckmann et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — Amino acids in Cse4 that are posttranslationally modified are evolutionarily conserved. (A) Cse4 is phosphorylated, methylated, and acetylated. The peptides identified by mass spectrometry are underlined, and the modified amino acid residues indicated (also see Table 1). The essential N-terminal domain (END) is shaded (amino acids 28–60). (B) The region containing the PTM sites within the Cse4 N-terminus is conserved. ClustalW alignment of the Cse4 END regions of point centromere yeasts. Alignment in logo format is shown at the bottom (Schneider and Stephens, 1990).