Expression of sigma 54 (ntrA)-dependent genes is probably united by a common mechanism.

Kustu, Sydney; Santero, E; Keener, John; Popham, D; Weiss, David S.

doi:10.1128/mmbr.53.3.367-376.1989

Cited by 297 publications

(165 citation statements)

References 75 publications

(113 reference statements)

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“…NifA proteins have the typical three-domain structure of c N -dependent transcription activators [4]. The central and C-terminal domains are highly conserved and are responsible for interaction with the c N -RNA polymerase and DNA binding, respectively [5,6]. Despite the similar structural organization of the NifA proteins among diazotrophs, the amino acid sequence of the N-terminal domain is poorly conserved and its function has not yet been ¢rmly established.…”

Section: Introductionmentioning

confidence: 99%

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

Monteiro

1999

FEMS Microbiology Letters

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The NifA protein is responsible for transcription activation of nif genes in the endophytic diazotroph Herbaspirillum seropedicae. When expressed in Escherichia coli this NifA protein is unable to activate the transcription of a Klebsiella pneumoniae nifH: :lacZ fusion. However, a form of NifA lacking the N-terminal domain did activate transcription and its activity was not inhibited by ammonium. In this work we show that when expressed separately, the N-terminal domain of H. seropedicae NifA protein can restore ammonium control of the N-truncated NifA activity in E. coli. This effect is dependent on the relative concentrations of the N-terminal domain and the N-truncated protein and suggests that the N-terminal domain behaves in this respect in a manner similar to that of NifL of the Q proteobacteria. ß

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Section: Introductionmentioning

confidence: 99%

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

Monteiro

1999

FEMS Microbiology Letters

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“…While the majority of the 'house-keeping genes' are tran-scribed by RNA polymerase holoenzyme (E0-70) containing the major 0-factor RpoD, expression of genes involved in the adaptation to environmental stimuli is often controlled by one of several alternative or factors. The RpoN o-factor (NtrA, o -s4) has been shown to be required for the expression of genes involved in various physiological functions [1]. Promoters recognized by 0 -54 always contain conserved GG and GC residues located 24 and 12 base pairs (bp), respectively, upstream of the transcriptional start point.…”

Section: Introductionmentioning

confidence: 99%

Regulation of the rpoN, ORF102 and ORF154 genes in Pseudomonas putida

KOHLER¹

1994

FEMS Microbiology Letters

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The DNA sequence downstream of the Pseudomonas putida rpoN gene and the adjacent ORF102 was determined. This region encodes an ORF (ORF154) whose gene product was found to be homologous to a family of phosphotransferases. Insertional mutagenesis and analysis of mRNA transcripts showed that the rpoN gene is transcribed separately from the two downstream genes. The rpoN promoter was localized to an 86 nucleotide-long region upstream of the rpoN gene by examination of the expression of a series of rpoN::lacZ fusions. The expression of rpoN in P. putida was independent of the nitrogen status of the cell but was 5 times higher in the rpoN mutant than in the wild-type strain, suggesting that the expression of the rpoN gene in this organism is autoregulated.

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“…All known ©^''-dependent promoters are subject to positive control, and transcription initiation by RNA polymerase containing o^"* is totally dependent on an activator protein. These activators normally bind to sites upstream of the promoter and, in two cases (NtrC and NifA), the activators have been shown to catalyse the isomerization of closed complexes between a^ holoenzyme and the promoter to transcriptionally productive open complexes (for reviews see Kustu et al, 1989 andThony andHennecke, 1989).…”

Section: Introductionmentioning

confidence: 99%

Cassette mutagenesis implicates a helix‐turn‐helix motif in promoter recognition by the novel RNA polymerase Sigma factor σ⁵⁴

Coppard

Merrick

1991

Molecular Microbiology

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Cassette mutagenesis has been used to study the role of a helix-turn-helix (HTH) motif in the novel RNA polymerase sigma factor sigma 54 of Klebsiella pneumoniae. Of the four residues which are predicted to be solvent-exposed in the second helix, the first (Glu-378) tolerated all substitutions, and some mutations of this residue increased expression from sigma 54-dependent promoters. Certain substitutions in the third exposed residue (Ser-382) produced a promoter-specific phenotype and all substitutions in the fourth residue (Arg-383) inactivated the protein, identifying this residue as being likely to be involved in base-specific interactions with the promoter. In vivo footprinting indicated that the inactive HTH mutants of sigma 54 were defective in interaction with both the -24 and -12 regions of the glnAp2 promoter.

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Expression of sigma 54 (ntrA)-dependent genes is probably united by a common mechanism.

Cited by 297 publications

References 75 publications

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

Regulation of the rpoN, ORF102 and ORF154 genes in Pseudomonas putida

Cassette mutagenesis implicates a helix‐turn‐helix motif in promoter recognition by the novel RNA polymerase Sigma factor σ⁵⁴

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Expression of sigma 54 (ntrA)-dependent genes is probably united by a common mechanism.

Cited by 297 publications

References 75 publications

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain

Regulation of the rpoN, ORF102 and ORF154 genes in Pseudomonas putida

Cassette mutagenesis implicates a helix‐turn‐helix motif in promoter recognition by the novel RNA polymerase Sigma factor σ54

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Cassette mutagenesis implicates a helix‐turn‐helix motif in promoter recognition by the novel RNA polymerase Sigma factor σ⁵⁴