FIG. 8.

(A) −2/+2 sites can overlap FHA-binding motifs. FHA1- and FHA2-binding motifs identified by using peptide libraries (12) were aligned with the known FHA1-binding motifs of p53 (10) and Rad9 (62), the known FHA2-binding motifs of Rad9 (7, 47), and the putative FHA2-binding motifs adjacent to the mapped −2/+2 sites of Swi6. Boxed residues are similar or identical to the ones identified by using peptide libraries in (12). Black circles over serine or threonine residues mark the known Chk2 phosphorylation site in p53 (S20), and the known Rad53 phosphorylation sites in Swi6. In Rad9, gray circles show serine or threonine residues that lie within matches to the −2/+2 consensus and could be phosphorylated by Rad53.