| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
134-197 |
DRI_Approach |
denotes |
DNA mismatch repair is initiated by either the Msh2-Msh6 or the |
| T2 |
216-240 |
DRI_Approach |
denotes |
recognition heterodimer. |
| T3 |
241-462 |
DRI_Approach |
denotes |
Here we optimized the expression and purification of Saccharomyces cerevisiae Msh2-Msh3 and performed a comparative study of Msh2-Msh3 and Msh2-Msh6 for mispair binding, sliding clamp formation, and Mlh1-Pms1 recruitment. |
| T4 |
463-730 |
DRI_Approach |
denotes |
Msh2-Msh3 formed sliding clamps and recruited Mlh1-Pms1 on +1, +2, +3, and +4 insertion/deletions and CC, AA, and possibly GG mispairs, whereas Msh2-Msh6 formed mispair-dependent sliding clamps and recruited Mlh1-Pms1 on 7 of the 8 possible base:base mispairs, the +1 |
| T5 |
757-808 |
DRI_Approach |
denotes |
, and to a low level on the +2 but not the +3 or +4 |
| T6 |
837-863 |
DRI_Approach |
denotes |
and not on the CC mispair. |
| T7 |
864-1094 |
DRI_Challenge |
denotes |
The mispair specificity of sliding clamp formation and Mlh1-Pms1 recruitment but not mispair binding alone correlated best with genetic data on the mispair specificity of Msh2-Msh3- and Msh2-Msh6-dependent mismatch repair in vivo. |
| T8 |
1095-1501 |
DRI_Approach |
denotes |
Analysis of an Msh2-Msh6/Msh3 chimeric protein and mutant Msh2-Msh3 complexes showed that the nucleotide binding domain and communicating regions but not the mispair binding domain of Msh2-Msh3 are responsible for the extremely rapid dissociation of Msh2-Msh3 sliding clamps from DNA relative to that seen for Msh2-Msh6, and that amino acid residues predicted to stabilize Msh2-Msh3 interactions with bent, |
| T9 |
1538-1647 |
DRI_Approach |
denotes |
DNA are more critical for the recognition of small +1 insertion/deletions than larger +4 insertion/deletions. |
