ArticleJournal of bacteriology2026
Ribonucleotide reductase repression: a mutational study of NrdR-binding motifs.
Article in Journal of bacteriology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 authors.
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Abstract
The prevalent transcriptional repressor NrdR binds to highly conserved sequences in the promoter regions of prokaryotic operons encoding the essential enzyme ribonucleotide reductase. The NrdR-binding sites consist of two partially palindromic 16 bp sequences (NrdR boxes) separated by a 15-16 bp linker sequence. We have assessed the requirement of both boxes for binding, the propensity of different NrdRs to bind to heterologous binding sites, and that the linker sequence is only limited to length and not sequence conservation. As we have observed several deviations from the conserved sequences of the NrdR boxes, we have tested the conservation requirements of individual base pairs in the NrdR boxes using a synthetic DNA fragment (Synt DNA) to which the NrdR proteins from the actinomycete
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