7p8v › Citations

MutL binds to 3' resected DNA ends and blocks DNA polymerase access.

Figure 1.
Figure 2.
Figure 3.
Borsellini A, Lebbink JHG, Lamers MH
OpenAccess logo Nucleic Acids Res (2022)
Cited: 4 times
EuropePMC logo PMID: 35670670

Abstract

DNA mismatch repair removes mis-incorporated bases after DNA replication and reduces the error rate a 100-1000-fold. After recognition of a mismatch, a large section of up to a thousand nucleotides is removed from the daughter strand followed by re-synthesis. How these opposite activities are coordinated is poorly understood. Here we show that the Escherichia coli MutL protein binds to the 3' end of the resected strand and blocks access of Pol I and Pol III. The cryo-EM structure of an 85-kDa MutL-DNA complex, determined to 3.7 Å resolution, reveals a unique DNA binding mode that positions MutL at the 3' end of a primer-template, but not at a 5' resected DNA end or a blunt DNA end. Hence, our work reveals a novel role for MutL in the final stages of mismatch repair by preventing premature DNA synthesis during removal of the mismatched strand.

Articles - 7p8v mentioned but not cited (1)

  1. MutL binds to 3' resected DNA ends and blocks DNA polymerase access. Borsellini A, Lebbink JHG, Lamers MH. Nucleic Acids Res 50 6224-6234 (2022)


Articles citing this publication (3)

  1. A conserved motif in the disordered linker of human MLH1 is vital for DNA mismatch repair and its function is diminished by a cancer family mutation. Wolf K, Kosinski J, Gibson TJ, Wesch N, Dötsch V, Genuardi M, Cordisco EL, Zeuzem S, Brieger A, Plotz G. Nucleic Acids Res 51 6307-6320 (2023)
  2. Insights into DNA cleavage by MutL homologs from analysis of conserved motifs in eukaryotic Mlh1. Putnam CD, Kolodner RD. Bioessays 45 e2300031 (2023)
  3. The mismatch repair endonuclease MutLα tethers duplex regions of DNA together and relieves DNA torsional tension. Witte SJ, Rosa IM, Collingwood BW, Piscitelli JM, Manhart CM. Nucleic Acids Res 51 2725-2739 (2023)


Quick links