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- W2153638961 abstract "Plasmid pAL5000 fromMycobacterium fortuitumencodes two proteins necessary for replication: RepA (307 amino acid residues) and RepB (119 residues). A single RNA species encoding these proteins was characterized, and its 5*end was defined. The proteins were expressed as maltose-binding protein fusions inEscherichia coli. The RepB protein was shown in vitro to bind specifically to a previously defined 435-bp region of pAL5000 containing the origin of replication (ori). The precise RepB binding sites were defined by DNase I footprinting experiments. RepB binds to two motifs in theoriregion: a high-affinity site within its own promoter region, implyingautoregulationofitsexpression,andalow-affinitysitefurtherupstream,presumablytheoriginofreplication itself. The binding to the latter motif seems to occur on one DNA strand only. The high-affinity binding site contains several palindromic sequences. Gel retardation assays were performed with the different binding sites as templates, and the binding constant to each site was estimated from protein titrations. This is thefirst molecular dissection of mycobacterial DNA-binding proteins and their interactions with their targets." @default.
- W2153638961 created "2016-06-24" @default.
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- W2153638961 date "1996-01-01" @default.
- W2153638961 modified "2023-09-27" @default.
- W2153638961 title "Protein-DNA Interactions in theoriRegion of the Mycobacterium fortuitumPlasmid pAL5000" @default.
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