Inhibition of RecA-mediated cleavage in covalent dimers of UmuD.
AUTOR(ES)
Lee, M H
RESUMO
Disulfide-cross-linked UmuD2 derivatives were cleaved poorly upon incubation with activated RecA. Reducing the disulfide bonds prior to incubating the derivatives with RecA dramatically increased their extent of cleavage. These observations suggest that the UmuD monomer is a better substrate for the RecA-mediated cleavage reaction than the dimer.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=178647Documentos Relacionados
- Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis.
- RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation.
- Mutations in bacteriophage lambda repressor that prevent RecA-mediated cleavage.
- RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis.
- Specific cleavage of DNA molecules at RecA-mediated triple-strand structure
