A thermostable protein factor acting on in vitro DNA transcription

Jacquet, Michel; Cukier-Kahn, Regine; Pla, Jesús; Gros, François

doi:10.1016/0006-291x(71)90204-x

Cited by 74 publications

(39 citation statements)

References 10 publications

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“…The Escherichia coli nucleoid-associated protein H-NS, originally identified as a heat stable transcription factor (1), is one of the major components of the bacterial nucleoid (2,3). It was therefore proposed to be involved in the structural organization of the E. coli chromosome.…”

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Structural Basis for H-NS-mediated Trapping of RNA Polymerase in the Open Initiation Complex at the rrnB P1

Dame

Wyman

Wurm

et al. 2002

Journal of Biological Chemistry

163

138

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The Escherichia coli H-NS protein is a nucleoid-associated protein involved in both transcription regulation and DNA compaction. Each of these processes involves H-NS-mediated bridge formation between adjacent DNA helices. With respect to transcription regulation, preferential binding sites in the promoter regions of different genes have been reported, and generally these regions are curved. Often H-NS binding sites overlap with promoter core regions or with binding sites of other regulatory factors. Not in all cases, however, transcriptional repression is the result of preferential binding by H-NS to promoter regions leading to occlusion of the RNA polymerase. In the case of the rrnB P1, H-NS actually stimulates open complex formation by forming a ternary RNAP⅐H-NS⅐DNA complex, while simultaneously stabilizing it to such an extent that promoter clearance cannot occur. To define the mechanism by which H-NS interferes at this step in the initiation pathway, the architecture of the RNAP⅐H-NS⅐DNA complex was analyzed by scanning force microscopy (SFM). The SFM images show that the DNA flanking the RNA polymerase in open initiation complexes is bridged by H-NS. On the basis of these data, we present a model for the specific repression of transcription initation at the rrnB P1 by H-NS.

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“…To identify the molecular mechanism underlying this novel kind of H-NS-mediated repression, we have analyzed RNAP⅐H-NS⅐DNA complexes by SFM. 1 …”

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confidence: 99%

Structural Basis for H-NS-mediated Trapping of RNA Polymerase in the Open Initiation Complex at the rrnB P1

Dame

Wyman

Wurm

et al. 2002

Journal of Biological Chemistry

163

138

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“…This DNA-binding protein is one of the most abundant proteins associated with the bacterial chromosome (reviewed in Ussery et al, 1994). Initially described as a transcription factor (Jacquet et al, 1971), this protein was later shown to play a role in organizing chromosomal DNA because of its ability to compact it (Spassky et al, 1984). In addition, curved DNA is generally the preferential target for binding of H-NS (Yamada et al, 1990).…”

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Role of Escherichia Coli Histone‐Like Nucleoid‐Structuring Protein in Bacterial Metabolism and Stress Response

Laurent‐Winter

Ngo

Danchin

et al. 1997

European Journal of Biochemistry

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The histone-like nucleoid-structuring protein, H-NS, is a major bacterial chromatin component which influences DNA structure and gene expression. Mutations in hns, the structural gene of H-NS protein, have been shown to result in highly pleiotropic effects in E.wherichiu coli cells. In this study, we have initiated an index of the proteins whose synthesis is, directly or indirectly regulated by H-NS. Using twodimensional gel electrophoresis, we have examined the global changes in gene expression which occured in an hns background compared with its wild-type parent. In addition, we analysed the effects of mutations in two other genes i.e. lrp and ptu, which are also involved in global regulatory pathways. Although these comparative analyses revealed several common differences, thus suggesting possible interactions between these regulatory mechanisms, i.e. H-NS, Lrp (leucine-responsive regulatory protein) and acetylphosphate, the most extensive modifications occurred in an hns mutant. Among the polypeptides whose level of synthesis was specifically altered in an hns mutant, several corresponded to H-NS targets previously identified by classical selection methods. Moreover, the present study allows us to characterize several H-NS targets, which were identified either by comparison with the E. coli two-dimensional reference maps or by microsequencing procedure. Many of these newly identified polypeptides are involved in adaptation of E. coli cells to environmental challenges, and one of them could be involved in bacterial virulence. Finally, synthesis of several proteins belonging to the heat-shock regulon, more particularly molecular chaperones, was induced in an hns mutant.

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“…The H-NS protein was isolated for the first time from Escherichia coli as a contaminant in RNA polymerase preparations (Jacquet et al, 1971). A few years later, on the basis of nucleotide sequence homology, H-NS proteins were identified by different groups in other enteric or related bacteria such as Proteus mirabilis, Serratia marcescens, Salmonella typhimurium and Erwinia chrysanthemi (Ussery et al, 1994).…”

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confidence: 99%