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• W2115958650 abstract "Summary L isteria monocytogenes PdxR is a member of the poorly characterized but widespread group of MocR / GabR ‐type chimeric bacterial proteins that have DNA ‐binding and aminotransferase‐like domains. Using mutational analysis, real‐time RT ‐ PCR , transcriptional fusions, gel‐shift assays, DNase I footprinting, and in vitro transcription, it was shown that PdxR is a direct activator of the pdxST operon, transcribed divergently from pdxR and responsible for the de novo synthesis of pyridoxal 5′‐phosphate ( PLP ), the major active form of vitamin B 6 . PLP acts as an anti‐activator of PdxR and is the only effector required to reduce the activity of PdxR . PdxR is also a negative autoregulator, and its ability to repress is increased by PLP . A dyad‐symmetry sequence, which overlaps the −35 region of the pdxS promoter and lies downstream of the pdxR transcription start point, serves as an important element of the PdxR binding site. Unexpectedly, some mutations in this activator binding site, disrupting the dyad‐symmetry element, caused constitutive, B 6 ‐independent expression from the pdxS promoter. The data suggest that PdxR ‐like proteins, for which PLP plays just a signalling role, form a separate functional group among the MocR / GabR ‐type proteins." @default.
• W2115958650 created "2016-06-24" @default.
• W2115958650 creator A5045114852 @default.
• W2115958650 date "2014-05-05" @default.
• W2115958650 modified "2023-10-03" @default.
• W2115958650 title "Role of PdxR in the activation of vitamin B₆biosynthesis in<i>L</i><i>isteria monocytogenes</i>" @default.
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• W2115958650 doi "https://doi.org/10.1111/mmi.12618" @default.
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