The Helicobacter felis ftsH gene encoding an ATP-dependent metalloprotease can replace the Escherichia coli homologue for growth and phage λ lysogenization

Melchers, Klaus; Wiegert, Thomas; Buhmann, Anita; Postius, Stefan; Schäfer, Klaus; Schumann, Wolfgang

doi:10.1007/s002030050588

Cited by 8 publications

(6 citation statements)

References 13 publications

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“…The high expression of this gene at 2.5 m is consistent with the high PAR measured during sampling (1278 µmol photons m −2 s −1 at the surface; Pfreundt et al 2014). In addition to high irradiance and UV damage, other stressors may also impact SAR11 activity as we observed high, non-differential, expression of the GroES chaperone (Hightower 1991, Frydman 2001) and the AAA+ FtsH proteases that are essential for proteolysis of regulatory proteins under environmental stress (Deuerling et al 1995, Herman et al 1995, Melchers et al 1998. In bacteria, ftsH is involved in heat shock responses and in proteolysis of phage proteins (Langklotz et al 2012) (Table S5).…”

Section: Sar11supporting

confidence: 84%

Winter mixing impacts gene expression in marine microbial populations in the Gulf of Aqaba

Miller¹,

Pfreundt²,

Hou³

et al. 2017

Aquat. Microb. Ecol.

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In aquatic systems, changes in temperature and irradiance fundamentally characterize the water column and regulate microbial population structure and function. In systems with stable thermal stratification, the warm surface mixed layer is typically nutrient impoverished, limiting biological production. In periods of destratification, convective mixing of the water column exposes the microorganisms inhabiting these mixed systems to rapid variations in light availability and spectra. We explored the impact of winter deep-mixing (500 m deep mixed layer) on microbial communities from the surface (2.5 m) and the aphotic waters (440 m) in the Gulf of Aqaba by examining changes in both population composition and function via DNA and RNA sequencing. The greatest fraction of 16S sequences was assigned to Euryarchaeota, while metatranscriptomes were dominated by Synechococcus transcripts. Community composition was highly similar at both depths, yet transcription profiles differed. Phototrophic organisms found at the photic surface overexpressed genes related to catabolism and energy metabolism, while genes affiliated with biosynthesis were overexpressed at the aphotic depth. Similar transcriptional trends were observed in the non-photoautotrophs SAR11, Euryarchaeota, and Thaumarchaeota, with niche partitioning based on differential utilization of nitrogen and phosphorus occurring between the 2 archaeal groups. We did not detect upregulated expression of cyanobacterial genes indicative of mixotrophy or glycogen metabolism in the aphotic zone, suggesting they survive the aphotic period by utilizing photosynthates produced in the photic zone. Indications for a mixotrophic lifestyle were observed for prasinophytes, with genes related to phagocytosis overexpressed at the aphotic depth compared with the surface.

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Section: Sar11supporting

confidence: 84%

Winter mixing impacts gene expression in marine microbial populations in the Gulf of Aqaba

Miller¹,

Pfreundt²,

Hou³

et al. 2017

Aquat. Microb. Ecol.

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“…The only other sequences from H. felis that have been published to date are for a P-type ATPase encoded by the copAP operon (24) and for a nearby open reading frame with homology to the E. coli ftsH gene encoding an ATP-dependent metalloprotease (273). Both have closely related homologs in H. pylori.…”

Section: Helicobacter Felismentioning

confidence: 98%

Emergence of DiverseHelicobacterSpecies in the Pathogenesis of Gastric and Enterohepatic Diseases

2001

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Since Helicobacter pylori was first cultivated from human gastric biopsy specimens in 1982, it has become apparent that many related species can often be found colonizing the mucosal surfaces of humans and other animals. These other Helicobacter species can be broadly grouped according to whether they colonize the gastric or enterohepatic niche. Gastric Helicobacter species are widely distributed in mammalian hosts and are often nearly universally prevalent. In many cases they cause an inflammatory response resembling that seen with H. pylori in humans. Although usually not pathogenic in their natural host, these organisms serve as models of human disease. Enterohepatic Helicobacter species are an equally diverse group of organisms that have been identified in the intestinal tract and the liver of humans, other mammals, and birds. In many cases they have been linked with inflammation or malignant transformation in immunocompetent hosts and with more severe clinical disease in immunocompromised humans and animals. The purpose of this review is to describe these other Helicobacter species, characterize their role in the pathogenesis of gastrointestinal and enterohepatic disease, and discuss their implications for our understanding of H. pylori infection in humans

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“…The whole operon is under the control of a single promoter and is induced by addition of copper to the medium and by thermal upshift. Sequencing of the same region from the chromosome of H. felis revealed a comparable genomic organization [30].…”

Section: Genomic Organization Of Ftsh Genesmentioning

confidence: 99%

FtsH – a single-chain charonin?

Schumann¹

1999

FEMS Microbiol Rev

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The ftsH gene encodes an ATP- and Zn(2+)-dependent metalloprotease with a molecular mass of about 70 kDa. It was first identified in Escherichia coli where it is also designated hflB, tolZ or mrsC, and seems to be present in most if not all bacteria. The FtsH protein is anchored to the cytoplasmic membrane via two transmembrane regions in such a way that the very short amino- and the long carboxy-termini are exposed into the cytoplasm. FtsH is member of the AAA family (ATPases associated with a variety of cellular activities) which are characterized by a module of about 200 amino acid residues in length containing an ATP-binding site. In Escherichia coli, FtsH forms a complex with a pair of periplasmically exposed membrane proteins, HflK and HflC. The E. coli enzyme is required for proteolytic degradation of some unstable proteins that include both soluble regulatory proteins such as sigma 32 (heat-shock sigma factor) and phage lambda CII (transcriptional activator), and membrane proteins including uncomplexed forms of SecY (forms the translocon together with SecE and SecG) and the a subunit of the F0 complex of the H(+)-ATPase. Its activity can be modulated by the HflKC proteins, by another membrane protein designated YccA which can transiently associate with both the FtsH and the HflKC proteins, or by small peptides such as CIII encoded by phage lambda (involved in lysogenization) or SpoVM (needed for sporulation) encoded by Bacillus subtilis. Besides being a protease, there is circumstantial evidence that FtsH also acts as a molecular chaperone. It influences protein assembly in and through the cytoplasmic membrane and associates with denatured alkaline phosphatase without degrading it. Therefore, FtsH may serve to maintain quality control of some cytoplasmic and membrane proteins. Such ATP-dependent proteases with intrinsic chaperone activity have been designated charonins.

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The Helicobacter felis ftsH gene encoding an ATP-dependent metalloprotease can replace the Escherichia coli homologue for growth and phage λ lysogenization

Cited by 8 publications

References 13 publications

Winter mixing impacts gene expression in marine microbial populations in the Gulf of Aqaba

Winter mixing impacts gene expression in marine microbial populations in the Gulf of Aqaba

Emergence of DiverseHelicobacterSpecies in the Pathogenesis of Gastric and Enterohepatic Diseases

FtsH – a single-chain charonin?

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