Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Nuclear-magnetic-resonance studies on nucleoprotein and histone phi 1-DNA complexes from marine invertebrate sperm

Proton magnetic resonance and other measurements have been carried out in order to study the behaviour of the lysine-rich histones phi 1 in the sperm chromatin of certain marine invertebrates. Well defined particles (12 S) have been obtained from this chromatin by nuclease treatment. Chromatin solubility as a function of ionic strength shows a relaxation at salt concentrations higher than in the case of calf thymus nucleoprotein. Nuclear magnetic resonance (NMR) studies show that the release of histone from DNA occurs both in chromatin and in the reconstituted complexes at practically the same ionic strength as solubility relaxation. The higher the arginine content of a given phi 1, the higher the ionic strength at which both effects take place. The NMR results demonstrate that arginine residues are bound more strongly than lysine residues. The data overall show that phi 1 histones play a role in the contraction mechanism of sperm chromatin similar to that of H 1 histone in calf thymus chromatin. The highly contracted state of sperm chromatin is directly related to the increased arginine content of the phi 1 histone.     

Oropharyngeal control of drinking in rats

Drinking was studied in water-deprived rats with chronic intragastric fistulas. Sham drinking, by which the ingested water was immediately lost through the open gastric fistula, was approximately four times greater than normal drinking. This proportion held across different levels of water deprivation, following 5-ml intragastric preloads of water or isotonic saline or ingestion of isotonic saline. The contribution of oropharyngeal controls in the normal drinking of rats is discussed and is compared with that of other species.     

The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family

A physiological role for paraoxonase (PON1) is still uncertain, but it catalyzes the hydrolysis of toxic organophosphates. Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here. Human PON1 and PON2 each have nine exons, and the exon/intron junctions occur at equivalent positions. PON1 and PON2 genes are both on chromosome 7 in human and on chromosome 6 in the mouse. Turkey and chicken, like most birds, lack paraoxonase activity and are very susceptible to organophosphates. However, they have a PON-like gene with approximately 70% identity with human PON1, PON2, and PON3. Another unexpected finding is that the deduced amino acid sequences of PON2 in human, mouse, dog, turkey, and chicken and of human PON3 are all missing the amino acid residue 105, which is lysine in human PON1. The expanded number of PON genes will have important implications for future experiments designed to discover the individual functions, catalytic properties, and physiological roles of the paraoxonases.