Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair (Q27629464)

2

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K Rausch

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P Hsieh

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W Yang

The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs

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publication date

January 2001

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published in

Molecular Cell

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volume

7

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issue

1

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page(s)

1-12

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cites work

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Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.

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MutS mediates heteroduplex loop formation by a translocation mechanism

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Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis

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Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

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Identification and characterization of a thermostable MutS homolog from Thermus aquaticus

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Heteroduplex DNA and ATP induced conformational changes of a MutS mismatch repair protein from Thermus aquaticus

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Modulation of MutS ATP hydrolysis by DNA cofactors

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

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7 January 2021

A phylogenomic study of the MutS family of proteins

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Mismatch repair, molecular switches, and signal transduction

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Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems

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The Human Mismatch Recognition Complex hMSH2-hMSH6 Functions as a Novel Molecular Switch

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hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA

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ATP-dependent Assembly of a Ternary Complex Consisting of a DNA Mismatch and the Yeast MSH2-MSH6 and MLH1-PMS1 Protein Complexes

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ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans

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Origin of the genetic code: a testable hypothesis based on tRNA structure, sequence, and kinetic proofreading

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Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

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Crystal structure of the ATP-binding subunit of an ABC transporter

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hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha

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7 January 2021

Replication errors: cha(lle)nging the genome

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Eukaryotic mismatch repair: an update

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Subunit interactions in ABC transporters: towards a functional architecture

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ATP-hydrolysis-dependent conformational switch modulates the stability of MutS-mismatch complexes

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Biochemistry and genetics of eukaryotic mismatch repair

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Eukaryotic DNA mismatch repair

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

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Mismatch repair in replication fidelity, genetic recombination, and cancer biology

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

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Processing of X-ray diffraction data collected in oscillation mode

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Repair of DNA heteroduplexes containing small heterologous sequences in Escherichia coli

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DNA repair: models for damage and mismatch recognition

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Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair

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7 January 2021

DNA-replication fidelity, mismatch repair and genome instability in cancer cells

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Switches, latches, and amplifiers: common themes of G proteins and molecular motors

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Dissociation of mismatch recognition and ATPase activity by hMSH2-hMSH3

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11172706

1 reference

Consolidated OpenCitations Corpus – April 2017