| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-79 |
Sentence |
denotes |
hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA. |
| T2 |
80-456 |
Sentence |
denotes |
The DNA binding properties of hMutSalpha and hMutLalpha and complex formation of hMutSalpha with hMutLalpha and hMutLbeta were investigated using binding experiments on magnetic bead-coupled DNA substrates with nuclear extracts as well as purified proteins. hMutSalpha binding to homoduplex DNA was disrupted by lower NaCl concentrations than hMutSalpha binding to a mismatch. |
| T3 |
457-667 |
Sentence |
denotes |
ATP markedly reduced the salt resistance of hMutSalpha binding but hMutSalpha still retained affinity for heteroduplexes. hMutSalpha formed a complex with hMutLalpha and hMutLbeta on DNA in the presence of ATP. |
| T4 |
668-731 |
Sentence |
denotes |
This complex only formed on 81mer and not 32mer DNA substrates. |
| T5 |
732-892 |
Sentence |
denotes |
Complex formation was enhanced by a mismatch in the DNA substrate, and hMutLalpha and hMutLbeta were shown to enter the complex at different ATP concentrations. |
| T6 |
893-1014 |
Sentence |
denotes |
Purified hMutLalpha showed an intrinsic affinity for DNA, with a preference for single-stranded over double-stranded DNA. |