Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli

Wada, Morimasa; Kano, Yasunobu; Ogawa, Tomoya; Okazaki, Tuneko; Imamoto, Fumio

doi:10.1016/0022-2836(88)90357-9

Cited by 156 publications

(105 citation statements)

References 35 publications

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“…Once the Zring is established, late proteins like FtsK, FtsQ, FtsL, FtsW, FtsI and FtsN are assembled in a linear-dependent fashion. It has been shown that E. coli strains lacking both subunits of HU protein have cell division defects, demonstrating a filamentation phenotype (Wada et al, 1988). Although the precise mechanism causing cell filamentation has not been determined, this defect is likely to be due to changes in the expression of fts genes.…”

Section: Discussionmentioning

confidence: 99%

“…Yet, even with a wide variety of functional NAP homologues, E. coli cells lacking HU do exhibit a variety of growth defects. Strains with mutations in both the a and b-subunits have increased sensitivity to UV and ionizing radiation (Boubrik & Rouviere-Yaniv, 1995;Li & Waters, 1998;Miyabe et al, 2000), have a lethal phenotype following cold or heat shock (Giangrossi et al, 2002;Wada et al, 1988), are defective in cell division (Dri et al, 1991) and are altered in outermembrane protein composition (Painbeni et al, 1997). Recently, the HU regulon was determined in E. coli using transcription profiling of strains deficient in the alpha, beta, or both HU subunits (Oberto et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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The nucleoid-associated protein HUβ affects global gene expression in Porphyromonas gingivalis

et al. 2013

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HU is a non-sequence-specific DNA-binding protein and one of the most abundant nucleoidassociated proteins in the bacterial cell. Like Escherichia coli, the genome of Porphyromonas gingivalis is predicted to encode both the HUa (PG1258) and the HUb (PG0121) subunit. We have previously reported that PG0121 encodes a non-specific DNA-binding protein and that PG0121 is co-transcribed with the K-antigen capsule synthesis operon. We also reported that deletion of PG0121 resulted in downregulation of capsule operon expression and produced a P. gingivalis strain that is phenotypically deficient in surface polysaccharide production. Here, we show through complementation experiments in an E. coli MG1655 hupAB double mutant strain that PG0121 encodes a functional HU homologue. Microarray and quantitative RT-PCR analysis were used to further investigate global transcriptional regulation by HUb using comparative expression profiling of the PG0121 (HUb) mutant strain to the parent strain, W83. Our analysis determined that expression of genes encoding proteins involved in a variety of biological functions, including iron acquisition, cell division and translation, as well as a number of predicted nucleoid associated proteins were altered in the PG0121 mutant. Phenotypic and quantitative real-time-PCR (qRT-PCR) analyses determined that under iron-limiting growth conditions, cell division and viability were defective in the PG0121 mutant. Collectively, our studies show that PG0121 does indeed encode a functional HU homologue, and HUb has global regulatory functions in P. gingivalis; it affects not only production of capsular polysaccharides but also expression of genes involved in basic functions, such as cell wall synthesis, cell division and iron uptake. INTRODUCTIONPorphyromonas gingivalis is a Gram-negative obligate anaerobe belonging to the family Bacteroidaceae that persists as a natural member of the human oral microbiota. A shift in the microbial community leading to outgrowth of this anaerobe is directly linked to periodontitis, a chronic inflammatory disease that leads to destruction of the tissues supporting the gums and ultimately, exfoliation of the teeth (Choil et al., 1990;Dzink et al., 1988;Grossi et al., 1994;Lamont & Jenkinson, 2000;Moore et al., 1991). This commensal can colonize, invade and multiply within gingival epithelial cells, as well as penetrate into deeper epithelial cell layers, potentially releasing the whole organism and/or virulence factors into the bloodstream (reviewed by Yilmaz, 2008). In addition to its ability to cause disease in the oral cavity, there are data indicating a role in systemic disease, including its ability to invade vascular endothelial cells (Dorn et al., 2000(Dorn et al., , 2002Jandik et al., 2008) and to cause aggregation of platelets (Pham et al., 2002). For many pathogenic bacteria, surface polysaccharides play a key role in immune modulation et al., 1996). HU typically acts as an accessory protein in virtually all types of nucleoprotein-mediated processes (reviewed by...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The nucleoid-associated protein HUβ affects global gene expression in Porphyromonas gingivalis

et al. 2013

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“…Upon isolation of HU from this organism, -90% of the protein consists of the o43 heterodimer, but the remaining 10% is homodimers of ct2 and 12 (Rouviere-Yaniv and Kjeldgaard, 1979). These homodimers can also be functionally active in vivo, as became clear from the isolation of hupA (encoding HUca) and hupB (encoding HUO) single and double mutants (Wada et al, 1988a). The hupA or hupB single mutant does not exhibit any phenotype different from those of the isogenic wild-type strain.…”

Section: Introductionmentioning

confidence: 98%

“…The hupA or hupB single mutant does not exhibit any phenotype different from those of the isogenic wild-type strain. The hupA hupB double mutant, however, does show phenotypic defects such as filamentation, cold sensitivity (Wada et al, 1988a), failure to replicate Fplasmids (Wada et al, 1988b) and inability to support transposition of phage Mu (Kano et al, 1989 (Figure 3). However, when these lysates are mixed, a specific ihf binding activity is observed (Figure 3) ) also results in the formation of a complex which migrates at exactly the same position as the IHF -DNA complex.…”

Section: Introductionmentioning

confidence: 99%

The HimA and HimD subunits of integration host factor can specifically bind to DNA as homodimers.

et al. 1994

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“…By contrast, double mutants are severely enfeebled under some growth conditions (especially at temperatures at the extremes of the permissible range). Double mutants contain less ordered nucleoids and form both filamentous cells and anucleate cells (160,164,361). The value of the double mutants is that the roles of the HU proteins can be assessed in vivo rather than solely in model systems.…”

Section: Structure and Composition Of Chromosomesmentioning

confidence: 99%

Organization of the Bacterial Chromosome

Schumann

2006

Dynamics of the Bacterial Chromosome

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Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli

Cited by 156 publications

References 35 publications

The nucleoid-associated protein HUβ affects global gene expression in Porphyromonas gingivalis

The nucleoid-associated protein HUβ affects global gene expression in Porphyromonas gingivalis

The HimA and HimD subunits of integration host factor can specifically bind to DNA as homodimers.

Organization of the Bacterial Chromosome

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