SnapShot: DNA Mismatch Repair

@article{Larrea2010SnapShotDM,
  title={SnapShot: DNA Mismatch Repair},
  author={Andres A. Larrea and Scott A Lujan and Thomas A Kunkel},
  journal={Cell},
  year={2010},
  volume={141},
  pages={730-730.e1}
}
Mismatch Repair in Bacteria and Eukaryotes Mismatch repair in the bacterium Escherichia coli is initiated when a homodimer of MutS binds as an asymmetric clamp to DNA containing a variety of base-base and insertion-deletion mismatches. The MutL homodimer then couples MutS recognition to the signal that distinguishes between the template and nascent DNA strands. In E. coli, the lack of adenine methylation, catalyzed by the DNA adenine methyltransferase (Dam) in newly synthesized GATC sequences… 
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork
TLDR
It is proposed that MutS directly contacts the DNA replication machinery, causing a dynamic change in the organization of DnaE at the replication fork during MMR, establishing a striking and intimate connection between MMR and the replicating DNA polymerase complex in vivo.
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TLDR
The role of the Bacillus subtilis processivity clamp DnaN is investigated, and it is found that it serves as a platform for mismatch detection and coupling of repair to DNA replication.
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This work used papillation as a tool to search for B. anthracis new mutator strains and identified a spontaneous mutator that carries a minitransposon insertion in the BAS4289 locus, the first report of a RecD2 helicase being associated with MMR.
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TLDR
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.
The C-Terminal Domain of the MutL Homolog from Neisseria gonorrhoeae Forms an Inverted Homodimer
TLDR
The crystal structure of the C-terminal domain (CTD) of the MutL homolog of Neisseria gonorrhoeae (NgoL) determined to a resolution of 2.4 Å shows that the metal binding motif exists in a helical configuration and that four of the six conserved motifs in theMutL family, including the metalbinding site, localize together to form a composite active site.
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A further understanding of the EndoMS/NucS-mediated non-canonical mismatch repair (MMR) pathway may reveal new strategies to predict and fight drug resistance.
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TLDR
The functional structures ofMMREs, their genetic defects and associated disorders, and autoimmunity to MMREs are charted, including the recent data that was the first to analyze autoantibodies against all seven kinds of MM REs in systemic autoimmune diseases, including idiopathic inflammatory myopathies.
Trapping and visualizing intermediate steps in the mismatch repair pathway in vivo
TLDR
A discrete site on MutS that is occupied by MutL in Bacillus subtilis is identified, providing insights into the mechanism that MutS employs to recruit MutL, and the consequences that ensue when MutL recruitment is blocked.
DNA Repair Polymerases
TLDR
This review focuses on the role of the numerous prokaryotic and eukaryotic DNA polymerases identified to date in the major DNA repair pathways: base excision repair (BER), nucleotide excision repaired (NER), doublestrand break repair (DSBR), cross-link repair (CLR), and mismatch repair (MMR).
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