The DNA binding properties of the MutL protein isolated from Escherichia coli.
AUTOR(ES)
Bende, S M
RESUMO
The mutL gene of Escherichia coli, which is involved in the repair of mispaired and unpaired nucleotides in DNA, has been independently cloned and the gene product purified. In addition to restoring methyl-directed DNA repair in extracts prepared from mutL strains, the purified MutL protein binds to both double and single stranded DNA. The affinity constant of MutL for unmethylated single stranded DNA was twice that of its affinity constant for methylated single stranded DNA and methylated or unmethylated double stranded DNA. The binding of MutL to double stranded DNA was not affected by the pattern of DNA methylation or the presence of a MutHLS-repairable lesion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=333914Documentos Relacionados
- The Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA.
- Dominant negative mutator mutations in the mutL gene of Escherichia coli.
- Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium.
- Products of DNA mismatch repair genes mutS and mutL are required for transcription-coupled nucleotide-excision repair of the lactose operon in Escherichia coli.
- Site-specific protein modification to identify the MutL interface of MutH
