Functional reorganization and productivity of a water-limited annual plant community

Plant Ecology - Changes in plant community structure in response to environmental change can be defined as community reorganization. In water-limited regions, the size of annual plants is related...     

Camels' milk: for drinking only?

Camels' milk, women's milk and cows' milk were kept at 30 degrees C and refrigerated at 4 degrees C. This explains the necessity to immediately freeze milk if it needs to be kept even for a few days. Cows' milk remained good for days if stirred and then turned sour, enabling the making of cheeses and butter. Camels' milk did not sour at 4 degrees C for up to 3 months. This means that camels' milk is mainly good only for drinking, as was promised to this animal by the Prophet.     

Halide concentrations in camel plasma in various states of hydration

Instrumental epithermal neutron activation analysis was used in determining the halide concentration of camel serum. The halides determined were sodium, chloride, bromide, and iodide. Serum was examined when the camels had free access to drinking water, following 10 d of water restriction and 2 h following rapid rehydration. When the camels were dehydrated there was a “serum storage” of iodide. This confirms the decline in thyroid metabolism previously described (15). Following rehydration the thyroid metabolism returned to normal. Dehydration also increased the serum bromide concentrations. This could have a tranquilizing effect, abetting the decrease in metabolism. There were no changes in sodium or chloride metabolism. It is concluded that use of neutron activation will allow an analysis of halides for physiological research.     

Human genomic site-specific recombination catalyzed by coliphage HK022 integrase

It has been previously demonstrated that the wild type integrase (Int) protein of coliphage HK022 can catalyze site-specific recombination in human cells between attachment (att) sites that were placed on extrachromosomal plasmids. In the present report it is shown that Int can catalyze the site-specific recombination reactions in a human cell culture on the chromosomal level. These include integrative (attP x attB) as well as excisive (attL x attR) reactions each in two configurations. In the cis configuration both sites are on the same chromosome, in the trans configuration one site is on a chromosome and the other on an episome. The reactions in cis were observed without any selection force, using the green fluorescent protein (GFP) as a reporter. The reactions in trans could be detected only when a selection force was applied, using the hygromycin-resistant (Hyg(R)) phenotype as a selective marker. All reactions were catalyzed without the need to supply any of the accessory proteins that are required by Int in its Escherichia coli host. The versatility of the att sites may be an advantage in the utilization of Int to integrate plasmid DNA into the genome, followed by a partial exclusion of the integrated plasmid.     

The effect of mutations in the Xis-binding sites on site-specific recombination in coliphage HK022

Excisionase (Xis) is an accessory protein that is required for the excision of the related prophages lambda and HK022. Xis binds to two tandemly arranged binding sites (X1 and X2) on the P arm of the recombination sites attP and attR. Gel-retardation analyses and site-specific recombination assays were conducted on derivatives bearing site-directed mutations in the X1 and X2 sites of phage HK022. The results confirm the cooperative binding of Xis to its sites, showing that binding to X1 stimulates further binding to X2. The results also show that mutants affected in a single site are inactive in excision, whereas mutants affected in both sites, which show a complete absence of Xis binding, display significant excision activity. This restored activity is attributed to the interaction of Xis with Integrase, the protein that catalyzes the site-specific recombination reaction.     

Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.