![]() Sequence logos generated by Seq2Logo (ref) for alignments of SHIP box 1, SHIPīox 2, and both SHIP boxes based on an alignment of 291 fungal species note cerevisiae Exo1 with closely relatedįungal species in the Saccharomycotina are displayed so that residues identical Sites, but not the Exo1-Mlh1 interaction. MIP box and the Mlh1 binding interaction. The Exo1-F447A,F448A variant disrupts the Exo1 Summary of yeast two-hybrid interactions with variousĮxo1 deletion constructs in prey vectors and their interactions with bait Our results identified two modes of Exo1 recruitment and a peptide module that mediates interactions between Msh2 and other proteins, and they support a model in which Exo1 functions in MMR by being tethered to the Msh2-Msh6 complex.Ī. The Remodeling of the Structure of Chromatin (Rsc) complex also functioned in both Exo1-dependent and Exo1-independent MMR in vivo. ![]() One of these, Fun30, had a small role in Exo1-dependent MMR in vivo. cerevisiae SHIP-box-containing proteins and three candidate human SHIP-box-containing proteins. ![]() ![]() The SHIP-Msh2 interactions were eliminated by the msh2 M470I mutation, and wild-type but not mutant SHIP peptides eliminated Exo1-dependent MMR in vitro. These three sites were redundant in Exo1-dependent MMR in vivo and could be replaced by a fusion protein between an N-terminal fragment of Exo1 and Msh6. We found that the unstructured C-terminal domain of Saccharomyces cerevisiae Exo1 contains two MutS homolog 2 (Msh2)-interacting peptide (SHIP) boxes downstream from the MutL homolog 1 (Mlh1)-interacting peptide (MIP) box. Eukaryotic DNA mismatch repair (MMR) involves both exonuclease 1 (Exo1)-dependent and Exo1-independent pathways. ![]()
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