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TitleUsing stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.
Journal, issue, pagesNucleic Acids Res, Vol. 41, Issue 17, Page 8166-8181, Year 2013
Publish dateJul 1, 2013
AuthorsFlora S Groothuizen / Alexander Fish / Maxim V Petoukhov / Annet Reumer / Laura Manelyte / Herrie H K Winterwerp / Martin G Marinus / Joyce H G Lebbink / Dmitri I Svergun / Peter Friedhoff / Titia K Sixma /
PubMed AbstractThe process of DNA mismatch repair is initiated when MutS recognizes mismatched DNA bases and starts the repair cascade. The Escherichia coli MutS protein exists in an equilibrium between dimers and ...The process of DNA mismatch repair is initiated when MutS recognizes mismatched DNA bases and starts the repair cascade. The Escherichia coli MutS protein exists in an equilibrium between dimers and tetramers, which has compromised biophysical analysis. To uncouple these states, we have generated stable dimers and tetramers, respectively. These proteins allowed kinetic analysis of DNA recognition and structural analysis of the full-length protein by X-ray crystallography and small angle X-ray scattering. Our structural data reveal that the tetramerization domains are flexible with respect to the body of the protein, resulting in mostly extended structures. Tetrameric MutS has a slow dissociation from DNA, which can be due to occasional bending over and binding DNA in its two binding sites. In contrast, the dimer dissociation is faster, primarily dependent on a combination of the type of mismatch and the flanking sequence. In the presence of ATP, we could distinguish two kinetic groups: DNA sequences where MutS forms sliding clamps and those where sliding clamps are not formed efficiently. Interestingly, this inability to undergo a conformational change rather than mismatch affinity is correlated with mismatch repair.
External linksNucleic Acids Res / PubMed:23821665 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution3.1 Å
Structure data

SASDA24: MutS tetramer (DNA mismatch repair protein MutS)
Method: SAXS/SANS

SASDAN3:
MutS dimer (DNA mismatch repair protein MutS, MutS)
Method: SAXS/SANS

SASDAQ3:
MutS tetramer (DNA mismatch repair protein MutS)
Method: SAXS/SANS

SASDAX3: MutS tetramer (DNA mismatch repair protein MutS)
Method: SAXS/SANS

SASDAY3: MutS tetramer (DNA mismatch repair protein MutS)
Method: SAXS/SANS

SASDAZ3: MutS tetramer (DNA mismatch repair protein MutS)
Method: SAXS/SANS

PDB-3zlj:
CRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTEIN MUTS D835R MUTANT IN COMPLEX WITH GT MISMATCHED DNA
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA COMPLEX / DIMER MUTANT / MISMATCH REPAIR / DNA REPAIR PROTEIN / DNA DAMAGE / NUCLEOTIDE-BINDING / ATP-BINDING

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