Enhanceosome assembly in eukaryotes often requires high mobility group A (HMGA) proteins. In prokaryotes, the only known transcriptional regulator with HMGA-like physical, structural and DNA-binding properties is Myxococcus xanthus CarD. Here, we report that every CarD-regulated process analysed also requires the product of gene carG, located immediately downstream of and transcriptionally coupled to carD. CarG has the zinc-binding H/C-rich metallopeptidase motif found in archaemetzincins, but with Q replacing a catalytically essential E. CarG, a monomer, binds two zinc atoms, shows no apparent metallopeptidase activity, and its stability in vivo absolutely requires the cysteines. This indicates a strictly structural role for zinc-binding. In vivo CarG localizes to the nucleoid but only if CarD is also present. In vitro CarG shows no DNA-binding but physically interacts with CarD via its N-terminal and not HMGA domain. CarD and CarG thus work as a single, physically linked, transcriptional regulatory unit, and if one exists in a bacterium so does the other. Like zinc-associated eukaryotic transcriptional adaptors in enhanceosome assembly, CarG regulates by interacting not with DNA but with another transcriptional factor.

Transcriptional factor CarD is the only reported prokaryotic analog of eukaryotic high-mobility-group A (HMGA) proteins, in that it has contiguous acidic and AT hook DNA-binding segments and multifunctional roles in Myxococcus xanthus carotenogenesis and fruiting body formation. HMGA proteins are small, randomly structured, nonhistone, nuclear architectural factors that remodel DNA and chromatin structure. Here we report on a second AT hook protein, CarD Sa , that is very similar to CarD and that occurs in the bacterium Stigmatella aurantiaca. CarD Sa has a C-terminal HMGA-like domain with three AT hooks and a highly acidic adjacent region with one predicted casein kinase II (CKII) phosphorylation site, compared to the four AT hooks and five CKII sites in CarD. Both proteins have a nearly identical 180-residue N-terminal segment that is absent in HMGA proteins. In vitro, CarD Sa exhibits the specific minor-groove binding to appropriately spaced AT-rich DNA that is characteristic of CarD or HMGA proteins, and it is also phosphorylated by CKII. In vivo, CarD Sa or a variant without the single CKII phosphorylation site can replace CarD in M. xanthus carotenogenesis and fruiting body formation. These two cellular processes absolutely require that the highly conserved N-terminal domain be present. Thus, three AT hooks are sufficient, the N-terminal domain is essential, and phosphorylation in the acidic region by a CKII-type kinase can be dispensed with for CarD function in M. xanthus carotenogenesis and fruiting body development. Whereas a number of hypothetical proteins homologous to the N-terminal region occur in a diverse array of bacterial species, eukaryotic HMGA-type domains appear to be confined primarily to myxobacteria.

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The ACD obtained presents a good safety profile, so would be a good alternative for treatment of cat allergy.

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An in vitro study was conducted using a model of reconstituted human corneal epithelial (SkinEthic™ HCE/Human Corneal Epithelium) to test the modulation of cytokines secretion activity of Pomanox® (PMX), a standardized commercial extract of pomegranate fruit characterized by high punicalagin α + β content. Cell viability and inhibition of the release of interleukin-8 (IL-8) was evaluated in four conditions: negative control, positive inflammatory control with lipopolysaccharide (LPS) from Escherichia coli, positive anti-inflammatory control (LPS plus dexamethasone), and LPS plus PMX after 24 h of culture. The mean (±standard error of mean (SEM)) IL-8 level was 48.7 ± 5.1 pg/mL in the PMX condition vs. 172.7 ± 19.3 and 26.6 ± 1.2 in the LPS from E. coli and negative control, respectively (p < 0.05) and 93.8 ± 8.7 pg/mL in LPS plus dexamethasone (p = 0.165). The percentages of inhibition of IL-8 release were 45.7% for LPS plus dexamethasone and 63.8% for LPS plus PMX. The percentage of cell viability (86%) was also higher for the LPS plus PMX condition. The present findings add evidence to the anti-inflammatory effect of a PMX in an in vitro model of reconstituted corneal epithelial cells.

Common millet (Panicum miliaceum L.) is a highly nutritious cereal used for human consumption, bird seed and/or ethanol production [1], in fact it is the sixth most consumed cereal worldwide: more than a third of the population takes millet from habitual way [2,3]. Although, nowadays, the grain is known in developed countries mainly as food for birds and livestock.The anaphylaxis produced by millet was first described in 1981 by Parker et al. [4], since then some cases have been described in which this cereal induces serious anaphylactic reactions after ingestion. In addition, millet also could act as an inhalant allergen described for the atopic bird keepers [5,6]. After the analysis of sera from bird keepers,