Annet Reumer
Netherlands Cancer Institute
5 Papers
47 Citations
Annet Reumer is an academic researcher from Netherlands Cancer Institute. The author has contributed to research in topics: MutS-1 & DNA mismatch repair. The author has an hindex of 4, co-authored 5 publications. Previous affiliations of Annet Reumer include University of Massachusetts Medical School.
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Papers
Chemical Trapping of the Dynamic MutS-MutL Complex Formed in DNA Mismatch Repair in Escherichia coli
Ines Winkler,Andreas D Marx,Damien Larivière,Roger J. Heinze,Michele Cristóvão,Michele Cristóvão,Annet Reumer,Ute Curth,Titia K. Sixma,Peter Friedhoff +9 more
TL;DR: Chemical cross-linking and fluorescence resonance energy transfer is used to study the interaction between MutS and MutL and to shed light onto the structure of this dynamic complex and identify the structural features of key events in DNA mismatch repair.
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Author response: MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA
Flora S. Groothuizen,Ines Winkler,Michele Cristóvão,Alexander Fish,Herrie H.K. Winterwerp,Annet Reumer,Andreas D Marx,Nicolaas Hermans,Robert A. Nicholls,Garib N. Murshudov,Joyce H.G. Lebbink,Peter Friedhoff,Titia K. Sixma +12 more
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Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS.
Joyce H.G. Lebbink,Joyce H.G. Lebbink,Alexander Fish,Annet Reumer,Ganesh Natrajan,Herrie H.K. Winterwerp,Titia K. Sixma +6 more
TL;DR: The G-proteins and MutS conceptually employ the same efficient use of the high energy cofactor: slow hydrolysis in the absence of a signal and fast conversion to the active state when required.
MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA
Flora S. Groothuizen,Ines Winkler,Michele Cristóvão,Alexander Fish,Herrie H.K. Winterwerp,Annet Reumer,Andreas D Marx,Nicolaas Hermans,Robert A. Nicholls,Garib N. Murshudov,Joyce H.G. Lebbink,Peter Friedhoff,Titia K. Sixma +12 more
TL;DR: This work explains how the sliding clamp promotes loading of MutL onto DNA, to activate downstream effectors, and elucidate a crucial mechanism that ensures that MMR is initiated only after detection of a DNA mismatch.
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation
Flora 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 +10 more
TL;DR: Structural data reveal that the tetramerization domains are flexible with respect to the body of the protein, resulting in mostly extended structures, and this inability to undergo a conformational change rather than mismatch affinity is correlated with mismatch repair.