PicR as a MarR Family Transcriptional Repressor Multiply Controls the Transcription of Picolinic Acid Degradation Gene Cluster
            <i>pic</i>
            in Alcaligenes faecalis JQ135

Xu, Siqiong; Wang, Xiao; Zhang, Fuyin; Jiang, Yinhu; Zhang, Yanting; Cheng, Minggen; Yan, Xin; Hong, Qing; He, Jian; Qiu, Jiguo

doi:10.1128/aem.00172-22

Cited by 9 publications

(4 citation statements)

References 54 publications

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“…The MarR proteins, a sub-group of winged helix-turn-helix (wHTH) DNA-binding proteins, regulate the expression of genes and play important roles in the regulation of diverse biological functions, such as resistance to multiple antibiotics, metabolism, biofilm formation, motility, and virulence in different pathogenic bacteria [25][26][27][28]. There are six members of the MarR family annotated in Aeromonas hydrophila ATCC 7966, encoded by the genes AHA_1240, AHA_2124, AHA_3609, AHA_1539, AHA_3721, AHA_0734, respectively.…”

Section: Discussionmentioning

confidence: 99%

Quantitative Proteomics Analysis Reveals the Effect of a MarR Family Transcriptional Regulator AHA_2124 on Aeromonas hydrophila

Li,

et al. 2023

Biology

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The transcriptional regulators of the MarR family play an important role in diverse bacterial physiologic functions, whereas their effect and intrinsic regulatory mechanism on the aquatic pathogenic bacterium Aeromonas hydrophila are, clearly, still unknown. In this study, we firstly constructed a deletion strain of AHA_2124 (ΔAHA_2124) of a MarR family transcriptional regulator in Aeromonas hydrophila ATCC 7966 (wild type), and found that the deletion of AHA_2124 caused significantly enhanced hemolytic activity, extracellular protease activity, and motility when compared with the wild type. The differentially abundant proteins (DAPs) were compared by using data-independent acquisition (DIA), based on a quantitative proteomics technology, between the ΔAHA_2124 strain and wild type, and there were 178 DAPs including 80 proteins up-regulated and 98 proteins down-regulated. The bioinformatics analysis showed that the deletion of gene AHA_2124 led to some changes in the abundance of proteins related to multiple biological processes, such as translation, peptide transport, and oxidation and reduction. These results provided a theoretical basis for better exploring the regulatory mechanism of the MarR family transcriptional regulators of Aeromonas hydrophila on bacterial physiological functions.

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Section: Discussionmentioning

confidence: 99%

Quantitative Proteomics Analysis Reveals the Effect of a MarR Family Transcriptional Regulator AHA_2124 on Aeromonas hydrophila

Li,

et al. 2023

Biology

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“…Some regulator protein can control multiple sites using one effector. For example, gentisate can induce GenR to activate transcriptions of two transcriptional units ( genD and genK ) in C. glutamicum , while 6‐hydroxypicolinic acid can derepress transcriptions of three transcriptional units ( picT , picB and picC ) from PicR in A. faecalis (Chao & Zhou, 2013; Xu, Wang, et al, 2022). Why are there multiple binding sites of DnfR in the dnf cluster with different effectors?…”

Section: Discussionmentioning

confidence: 99%

The MocR family transcriptional regulator DnfR has multiple binding sites and regulates Dirammox gene transcription in Alcaligenes faecalis JQ135

Wang

et al. 2022

Environmental Microbiology

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Microbial ammonia oxidation is vital to the nitrogen cycle. A biological process, called Dirammox (direct ammonia oxidation, NH3→NH2OH→N2), has been recently identified in Alcaligenes ammonioxydans and Alcaligenes faecalis. However, its transcriptional regulatory mechanism has not yet been fully elucidated. The present study characterized a new MocR‐like transcription factor DnfR that is involved in the Dirammox process in A. faecalis strain JQ135. The entire dnf cluster was composed of 10 genes and transcribed as five transcriptional units, that is, dnfIH, dnfR, dnfG, dnfABCDE and dnfF. DnfR activates the transcription of dnfIH, dnfG and dnfABCDE genes, and represses its own transcription. The intact 1506‐bp dnfR gene was required for activation of Dirammox. Electrophoretic mobility shift assays and DNase I footprinting analyses showed that DnfR has one binding site in the dnfH‐dnfR intergenic region and two binding sites in the dnfG‐dnfA intergenic region. Three binding sites of DnfR shared a 6‐bp repeated conserved sequence 5′‐GGTCTG‐N17‐GGTCTG‐3′ which was essential for the transcription of downstream target genes. Cysteine and glutamate act as possible effectors of DnfR to activate the transcription of transcriptional units of dnfG and dnfABCDE, respectively. This study provided new insights in the transcriptional regulation mechanism of Dirammox by DnfR in A. faecalis JQ135.

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“…The lower pathway was 2,5-dihydroxypyridine (2,5DHP) to fumaric acid (a Krebs cycle intermediate), which was catalyzes by four conserved enzymes, 2,5DHP 5,6-dioxygenase (PicD), N-formylmaleamic acid deformylase (PicE), maleamic acid amidohydrolase (PicF), and maleic acid isomerase (PicG). The pic gene cluster was predicted as widely distributed in α-, β-, and γ-Proteobacteria [13,18].…”

Section: Introductionmentioning

confidence: 99%

Expression and Characterization of 3,6-Dihydroxy-picolinic Acid Decarboxylase PicC of Bordetella bronchiseptica RB50

Yuan

Zhao

Tong³

et al. 2023

Microorganisms

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Picolinic acid (PA) is a typical mono-carboxylated pyridine derivative produced by human/animals or microorganisms which could be served as nutrients for bacteria. Most Bordetella strains are pathogens causing pertussis or respiratory disease in humans and/or various animals. Previous studies indicated that Bordetella strains harbor the PA degradation pic gene cluster. However, the degradation of PA by Bordetella strains remains unknown. In this study, a reference strain of genus Bordetella, B. bronchiseptica RB50, was investigated. The organization of pic gene cluster of strain RB50 was found to be similar with that of Alcaligenes faecalis, in which the sequence similarities of each Pic proteins are between 60% to 80% except for PicB2 (47% similarity). The 3,6-dihydroxypicolinic acid (3,6DHPA) decarboxylase gene (BB0271, designated as picCRB50) of strain RB50 was synthesized and over-expressed in E. coli BL21(DE3). The PicCRB50 showed 75% amino acid similarities against known PicC from Alcaligenes faecalis. The purified PicCRB50 can efficiently transform 3,6DHPA to 2,5-dihydroxypyridine. The PicCRB50 exhibits optimal activities at pH 7.0, 35 °C, and the Km and kcat values of PicCRB50 for 3,6DHPA were 20.41 ± 2.60 μM and 7.61 ± 0.53 S−1, respectively. The present study provided new insights into the biodegradation of PA by pathogens of Bordetella spp.

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PicR as a MarR Family Transcriptional Repressor Multiply Controls the Transcription of Picolinic Acid Degradation Gene Cluster pic in Alcaligenes faecalis JQ135

Abstract: The pic gene cluster was found to be responsible for PA degradation and widely distributed in Alpha- , Beta- , and Gammaproteobacteria . Thus, it is very necessary to understand the regulation mechanism of the pic cluster in these strains.

Cited by 9 publications

References 54 publications

Quantitative Proteomics Analysis Reveals the Effect of a MarR Family Transcriptional Regulator AHA_2124 on Aeromonas hydrophila

Quantitative Proteomics Analysis Reveals the Effect of a MarR Family Transcriptional Regulator AHA_2124 on Aeromonas hydrophila

The MocR family transcriptional regulator DnfR has multiple binding sites and regulates Dirammox gene transcription in Alcaligenes faecalis JQ135

Expression and Characterization of 3,6-Dihydroxy-picolinic Acid Decarboxylase PicC of Bordetella bronchiseptica RB50

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