2023
DOI: 10.1107/s2059798323001298
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A tetramerization domain in prokaryotic and eukaryotic transcription regulators homologous to p53

Abstract: Transcriptional regulation usually requires the action of several proteins that either repress or activate a promotor of an open reading frame. These proteins can counteract each other, thus allowing tight regulation of the transcription of the corresponding genes, where tight repression is often linked to DNA looping or cross-linking. Here, the tetramerization domain of the bacterial gene repressor Rco from Bacillus subtilis plasmid pLS20 (RcopLS20) has been identified and its structure is shown to share high… Show more

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Cited by 3 publications
(1 citation statement)
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“…In parallel, an anti-repressor, termed Rap, is held inactive through binding to a short quorum-sensing signaling peptide, Phr, encoded by the plasmid. The transition to an "ON" state is facilitated by a decrease in Phr concentration, and the consequent liberation of Rap, which counteracts Rco, thus promoting conjugation [23][24][25][26] .…”
Section: Introductionmentioning
confidence: 99%
“…In parallel, an anti-repressor, termed Rap, is held inactive through binding to a short quorum-sensing signaling peptide, Phr, encoded by the plasmid. The transition to an "ON" state is facilitated by a decrease in Phr concentration, and the consequent liberation of Rap, which counteracts Rco, thus promoting conjugation [23][24][25][26] .…”
Section: Introductionmentioning
confidence: 99%