ArticleGenes and environment : the official journal of the Japanese Environmental Mutagen Society2019
Purification and interactions of the MucA' and MucB proteins constituting the DNA polymerase RI.
Article in Genes and environment : the official journal of the Japanese Environmental Mutagen Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Common themes in architecture and interactions of prokaryotic PolB2 and Pol V mutasomes inferred fromComputational and structural biotechnology journal · 2025Article
- Effect of episomally encoded DNA polymerases on chemically induced mutagenesis at theGenes and environment : the official journal of the Japanese Environmental Mutagen Society · 2020Article
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4 authors.
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Abstract
backgroundThe MucA' and MucB proteins comprise the core of DNA polymerase RI which is a strong mutator utilized in mutagenicity assays such as the standard Ames test. A close relative DNA polymerase V, composed of the homologous UmuD' and UmuC proteins, is considered to be an ortholog of the mammalian DNA polymerase η. The catalytic subunits of these polymerases belong to the Y-family which specializes in the translesion DNA synthesis across various DNA adducts to rescue stalled chromosomal replication at the expense of mutations. Based on genetic evidence, DNA polymerase RI possesses the greatest ability to induce various types of mutations among all so far characterized members of the Y-superfamily. The exceptionally high mutagenic potential of MucA'B has been taken advantage of in numerous bacterial mutagenicity assays incorporating the conjugative plasmid pKM101 carrying the
resultsWe established new procedures for the purification of MucB protein as well as its accessory protein MucA' using the refolding techniques. The purified MucA' protein behaved as a molecular dimer which was fully stable in solution. The soluble monomeric form of MucB protein was obtained after refolding on a gel-filtration column and remained stable in a nondenaturing buffer containing protein aggregation inhibitors. Using the surface plasmon resonance technique, we demonstrated that the purified MucA' and MucB proteins interacted and that MucB protein preferentially bound to single-stranded DNA. In addition, we revealed that MucB protein interacted with the β-subunit of DNA polymerase III holoenzyme of
conclusionThe MucA' and MucB proteins can be isolated from inclusion bodies and solubilized in vitro. The refolded MucB protein interacts with its MucA' partner as well as with DNA what suggests it retains biological activity. The interaction of MucB with the processivity subunit of DNA polymerase III may imply the role of the subunit as an accessory protein to MucB during the translesion DNA synthesis.
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