Analysis of the human MutLalpha.MutSalpha complex (Q24300627)

MutS homolog 6

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MutL homolog 1

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PMS1 homolog 2, mismatch repair system component

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MutSalpha complex binding

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author

Stefan Zeuzem

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Albrecht Piiper

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object named as

Albrecht Piiper

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author name string

Guido Plotz

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Marc Wormek

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Jochen Raedle

Biochemical and Biophysical Research Communications

5

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language of work or name

English

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publication date

17 February 2006

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published in

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volume

340

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page(s)

852-9

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issue

3

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cites work

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Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair

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The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch

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DNA mismatch repair: MutS structures bound to mismatches.

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Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair

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The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair

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Mechanism of 5'-directed excision in human mismatch repair

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Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA.

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Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

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The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

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MutS and MutL activate DNA helicase II in a mismatch-dependent manner

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Mismatch-, MutS-, MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex

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DNA-dependent activation of the hMutSalpha ATPase

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Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism

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The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity

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Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit.

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Escherichia coli MutL loads DNA helicase II onto DNA.

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Interaction of Escherichia coli MutS and MutL at a DNA mismatch

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Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis

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DNA chain length dependence of formation and dynamics of hMutSalpha.hMutLalpha.heteroduplex complexes

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Mutations within the hMLH1 and hPMS2 subunits of the human MutLalpha mismatch repair factor affect its ATPase activity, but not its ability to interact with hMutSalpha

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Differential and simultaneous adenosine di- and triphosphate binding by MutS.

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Hydrolytically Deficient MutS E694A Is Defective in the MutL-dependent Activation of MutH and in the Mismatch-dependent Assembly of the MutS · MutL · Heteroduplex Complex

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Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites

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Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system.

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MutS mediates heteroduplex loop formation by a translocation mechanism

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Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD.

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ATP hydrolysis-dependent formation of a dynamic ternary nucleoprotein complex with MutS and MutL.

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hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA.

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N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha

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Mismatch repair, molecular switches, and signal transduction.

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An efficient method for the preparation of long heteroduplex DNA as substrate for mismatch repair by the Escherichia coli MutHLS system

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7 January 2021