Autoregulation of iclR, the gene encoding the repressor of the glyoxylate bypass operon

Gui, Lizhen; Sunnarborg, Alden; Pan, Bin; LaPorte, David C.

doi:10.1128/jb.178.1.321-324.1996

Cited by 60 publications

(62 citation statements)

References 26 publications

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“…However, the promoter region upstream of the TS1 site was similar to that of the E. coli ace operon, and contained a similar palindrome structure to that of the ace operon, to which its specific repressor protein, IclR, binds ( Fig. 5a) (Gui et al, 1996 ;Negre et al, 1992). The promoter region of icdI encoding acetate-inducible IDH-I isozyme of C. maris was also reported to resemble that of the E. coli ace operon (Ishii et al, 1993 ;Suzuki et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

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The cold-inducible icl gene encoding thermolabile isocitrate lyase of a psychrophilic bacterium, Colwellia maris a aThe GenBank accession number for the sequence reported in this paper is AB066287.

et al. 2002

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The gene encoding isocitrate lyase (ICL ; EC 4 . 1 . 3 . 1) of a psychrophilic bacterium, Colwellia maris, was cloned and sequenced. The ORF of the gene (icl) was 1584 bp long, and the predicted gene product consisted of 528 aa (molecular mass 58 150 Da) and showed low homology with the corresponding enzymes from other organisms. The analyses of amino acid content and primary structure of the C. maris ICL suggested that it possessed many features of a cold-adapted enzyme. Primer extension and Northern blot analyses revealed that two species of the icl mRNAs with differential lengths of 5'-untranslated regions (TS1 and TS2) were present, of which the 5' end (TS1 and TS2 sites) were G and A, located at 130 and 39 bases upstream of the translation start codon, respectively. The levels of TS1 and TS2 mRNAs were increased by both acetate and low temperature. The induction of icl expression by low temperature took place in the C. maris cells grown on succinate as the carbon source but not acetate. Furthermore, a similar manner of inductions was also found in the levels of the translation and the enzyme activity in cell-free extract. These results suggest that the icl gene, encoding thermolabile isocitrate lyase, of C. maris is important for acetate utilization and cold adaptation.

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Section: Discussionmentioning

confidence: 99%

“…4a) Inverted arrows indicate palindromic repeats. In aceB, this sequence is the IclR repressor binding site (Gui et al, 1996). The putative k35 and k10 promoter elements and the putative transcriptional start points (j1) are indicated by bold and boxed letters, respectively.…”

Section: Analysis Of 5h-terminal Region Of the C Maris Icl Mrnamentioning

confidence: 99%

The cold-inducible icl gene encoding thermolabile isocitrate lyase of a psychrophilic bacterium, Colwellia maris a aThe GenBank accession number for the sequence reported in this paper is AB066287.

et al. 2002

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“…E. coli IclR also forms a dimer and regulates both the aceBAK operon and its own expression. [30][31][32] Furuta et al 20 previously reported that the region between 100 and 274 a.a. of IclR is involved in dimerization and that this region can be replaced with other functional homodimerization domains (Figure 1). To design a high-throughput screening system targeting the WalR RR, we constructed a chimeric repressor gene consisting of sequences encoding the 100 amino-terminal amino acid residues of IclR that constitute the DNA-binding domain (N100) fused to the walR, arcA or ompR RR genes (Figure 2a).…”

Section: High-throughput Screening Of Inhibitors Targeting Walrmentioning

confidence: 99%

Novel antibacterial compounds specifically targeting the essential WalR response regulator

et al. 2010

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The WalK/WalR (YycG/YycF) two-component system, which is essential for cell viability, is highly conserved and specific to low-GC percentage of Gram-positive bacteria, making it an attractive target for novel antimicrobial compounds. Recent work has shown that WalK/WalR exerts an effect as a master regulatory system in controlling and coordinating cell wall metabolism with cell division in Bacillus subtilis and Staphylococcus aureus. In this paper, we develop a high-throughput screening system for WalR inhibitors and identify two novel inhibitors targeting the WalR response regulator (RR): walrycin A (4-methoxy-1-naphthol) and walrycin B (1,6-dimethyl-3-[4-(trifluoromethyl)phenyl]pyrimido [5,4-e][1,2,4]triazine-5,7-dione). Addition of these compounds simultaneously affects the expression of WalR regulon genes, leading to phenotypes consistent with those of cells starved for the WalK/WalR system and having a bactericidal effect. B. subtilis cells form extremely long aseptate filaments and S. aureus cells form large aggregates under these conditions. These results show that walrycins A and B are the first antibacterial agents targeting WalR in B. subtilis and S. aureus.

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“…Further studies revealed that IclR autologously represses transcription of iclR itself (Gui et al, 1996), and two different modes of repression have been proposed for repression of aceBAK transcription by IclR (Yamamoto & Ishihama, 2003).…”

Section: Introductionmentioning

confidence: 99%

Characterization of LgnR, an IclR family transcriptional regulator involved in the regulation of l-gluconate catabolic genes in Paracoccus sp. 43P

Shimizu

Nakamura

2014

Microbiology

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Five genes encoding enzymes required for L-gluconate catabolism, together with genes encoding components of putative ABC transporters, are located in a cluster in the genome of Paracoccus sp. 43P. A gene encoding a transcriptional regulator in the IclR family, lgnR, is located in front of the cluster in the opposite direction. Reverse transcription PCR analysis indicated that the cluster was transcribed as an operon, termed the lgn operon. Two promoters, P lgnA and P lgnR , are divergently located in the intergenic region, and transcription from these promoters was induced by addition of L-gluconate or D-idonate, a catabolite of L-gluconate. Deletion of lgnR resulted in constitutive expression of lgnA, lgnH and lgnR, indicating that lgnR encodes a repressor protein for the expression of the lgn operon and lgnR itself. Electrophoretic mobility shift assay and DNase I footprinting analyses revealed that recombinant LgnR binds to both P lgnA and P lgnR , indicating that LgnR represses transcription from these promoters by competing with RNA polymerase for binding to these sequences. D-Idonate was identified as a candidate effector molecule for dissociation of LgnR from these promoters. Phylogenetic analysis revealed that LgnR formed a cluster with putative proteins from other genome sequences, which is distinct from those proteins of known regulatory functions, in the IclR family of transcriptional regulators. Additionally, the phylogeny suggests an evolutionary linkage between the L-gluconate catabolic pathway and Dgalactonate catabolic pathways distributed in Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria and Actinobacteria.

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Autoregulation of iclR, the gene encoding the repressor of the glyoxylate bypass operon

Cited by 60 publications

References 26 publications

The cold-inducible icl gene encoding thermolabile isocitrate lyase of a psychrophilic bacterium, Colwellia maris a aThe GenBank accession number for the sequence reported in this paper is AB066287.

The cold-inducible icl gene encoding thermolabile isocitrate lyase of a psychrophilic bacterium, Colwellia maris a aThe GenBank accession number for the sequence reported in this paper is AB066287.

Novel antibacterial compounds specifically targeting the essential WalR response regulator

Characterization of LgnR, an IclR family transcriptional regulator involved in the regulation of l-gluconate catabolic genes in Paracoccus sp. 43P

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