Purification and characterization of the deoR repressor of Escherichia coli.

Mortensen, L.; Dandanell, Gert; Hammer, Karin

doi:10.1002/j.1460-2075.1989.tb03380.x

Cited by 72 publications

(63 citation statements)

References 23 publications

(38 reference statements)

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“…On the basis of this and the mutational analysis described herein, the most likely model for interaction of ComA proteins with the srfA promoter is shown in Fig. 2 (13) and the repression of the gal (11,18), lac (3, 10, 31), and deo (19) operons in Escherichia coli. In more complex cases, such as the araBAD operon, repression is mediated by DNA looping (9) and by arabinosemediated loop breaking when the operon is induced (17).…”

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confidence: 70%

Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis

Nakano

Zuber

1993

J Bacteriol

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confidence: 70%

Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis

Nakano

Zuber

1993

J Bacteriol

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“…His protein caused a complete mobility shift at the concentration of 90 pmol, a 90-fold molar excess that probably represented only a 10-fold molar excess of native protein, as purified DeoR-type repressors seemed to be mainly octamers (Zeng et al, 2000;Mortensen et al, 1989).…”

Section: Identification Of the Sugrmentioning

confidence: 99%

Regulation of ldh expression during biotin-limited growth of Corynebacterium glutamicum

et al. 2009

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Corynebacterium glutamicum is a biotin-auxotrophic bacterium and some strains efficiently produce glutamic acid under biotin-limiting conditions. In an effort to understand C. glutamicum metabolism under biotin limitation, growth of the type strain ATCC 13032 was investigated in batch cultures and a time-course analysis was performed. A transient excretion of organic acids was observed and we focused our attention on lactate synthesis. Lactate synthesis was due to the ldh-encoded l-lactate dehydrogenase (Ldh). Features of Ldh activity and ldh transcription were analysed. The ldh gene was shown to be regulated at the transcriptional level by SugR, a pleiotropic transcriptional repressor also acting on most phosphotransferase system (PTS) genes. Electrophoretic mobility shift assays (EMSAs) and site-directed mutagenesis allowed the identification of the SugR-binding site. Effector studies using EMSAs and analysis of ldh expression in a ptsF mutant revealed fructose 1-phosphate as a highly efficient negative effector of SugR. Fructose 1,6-bisphosphate also affected SugR binding.

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“…There was no indication of a second, upstream promoter like that found in the deo operon. Both cko promoters are overlapped by palindromic structures, which have been shown to act as binding sites for the deoR repressor [17,181. Also at the nupG promoter an overlapping palindromic structure is found (underlined in Fig.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the regulatory region of the Escherichia coli nupG gene, encoding a nucleoside‐transport protein

Munch‐Petersen

Jensen

1990

European Journal of Biochemistry

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The S1-mapping procedure, when applied to an 800-bp fragment upstream of the nupG structural gene of Escherichiu coli revealed one transcription-initiation site. The corresponding promoter is negatively regulated by the cj,tR and the deoR repressors. The expression of the gene is activated by the complex between CAMP and its receptor protein. In strains lacking cAMP the promoter expression is reduced and it is no longer regulated by the c y R repressor, whereas the deoR regulation is retained.Two high-affinity nucleoside-transport systems operate in the cells of E,rcherichia coli [l -41. They are termed the nupC and the nupG systems. The two systems differ in specificity: the nupC system transports nucleosides other than guanosine and deoxyguanosine, while the nupC system mediates the transport of all nucleosides. Both systems transport the nucleosides actively into the cell (for further references, see 141). It was shown previously that the nupC gene, located at 63 min on the E. coli chromosome, encodes a membranebound protein with a molecular mass of approximately 45 kDa. The sequence of the structural gene and of the regulatory region upstream of the gene has been determined [5].Expression of the nupG gene is under a double-negative control exerted by the cytR and deoR repressor proteins. Like other cytR-regulated transcriptional units, the synthesis is also activated by the cAMP receptor protein (CRP) control system. Two other E. coli loci are controlled negatively by cytR and deoR and positively by the CAMP-CRP complex. These are the deu operon [6] and the tsx gene(s) [7] (for further references, see [6]). In the regulatory region of the deu operon [8] and presumably also in the tsx gene [9] two promoters, P1 and P2, operate. In the deo operon, PI is controlled by the deoR repressor only, whereas P2 is subject to control by cytR and dcoR and in addition is stimulated by the CAMP-CRP complex. The two deo promoters are located 599 bp apart.In the present paper, the regulation of nupC has been quantified using protein fusions of the NH2 end of the nupG gene to the lacZ gene. The fused gene was cloned on singlecopy plasmids and introduced into strains with cytR and deoR mutations, with or without a Acya mutation. Different lengths of the regulatory region upstream of the structural gene were included in the cloned fragments in order to locate approximately the sites of regulation. S1 mapping indicated the presence of only one promoter site located 64 bp upstream of the structural gene. When present on plasmids in Acya strains, this promoter gives rise to

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Purification and characterization of the deoR repressor of Escherichia coli.

Cited by 72 publications

References 23 publications

Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis

Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis

Regulation of ldh expression during biotin-limited growth of Corynebacterium glutamicum

Analysis of the regulatory region of the Escherichia coli nupG gene, encoding a nucleoside‐transport protein

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