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The endonuclease domain of Bacillus subtilis MutL is functionally asymmetric.

Abstract：

:DNA mismatch repair is an evolutionarily conserved repair pathway that corrects replication errors. In most prokaryotes and all eukaryotes, the mismatch repair protein MutL is a sequence-unspecific endonuclease that nicks the newly synthesized strand and marks it for repair. Although the sequence of the endonuclease domain of MutL is not conserved, eukaryotic MutLα and prokaryotic MutL share four conserved motifs that define the endonuclease site of the protein. Their endonuclease activity is stimulated by the processivity sliding β-clamp, or its eukaryotic counterpart PCNA, highlighting the functional conservation. Bacterial MutL homologs form homodimers and, therefore, they have two endonuclease sites. However, eukaryotic MutL homologs associate to form heterodimers, where only one of the protomers of the dimer has endonuclease activity. To probe whether bacterial MutL needs its two endonuclease sites, we engineered variants of B. subtilis MutL harboring a single nuclease site and showed that these variants are functional nucleases. We also find that the protomer harboring the nuclease site must be able to bind to the β-clamp to recapitulate the nicking activity of wild-type MutL. These results demonstrate the functional asymmetry of bacterial MutL and strengthen the similarities with the endonuclease activity of eukaryotic MutL homologs.

journal_name

DNA Repair (Amst)

journal_title

DNA repair

authors

Liu L,Ortiz Castro MC,Rodríguez González J,Pillon MC,Guarné A

doi

10.1016/j.dnarep.2018.10.003

subject

Has Abstract

pub_date

2019-01-01 00:00:00

pages

1-6

eissn

1568-7864

issn

1568-7856

pii

S1568-7864(18)30146-0

journal_volume

73

pub_type

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