The nucleotide sequence of the luxA and luxB genes of Xenorhabdus luminescens HM and a comparison of the amino acid sequences of luciferases from four species of bioluminescent bacteria.

The luxA and luxB genes of bioluminescent bacteria encode the alpha and beta subunits of luciferase, respectively. Sequences of the luxA and luxB genes of Xenorhabdus luminescens, the only terrestrial bioluminescent bacterium known, were determined and the amino acid sequence of luciferase deduced. The alpha subunit was found to contain 360 amino acids and has a calculated molecular weight of 41,005 Da, while the beta subunit contains 327 amino acids and has a calculated molecular weight of 37,684 Da. Alignment of this luciferase with the luciferases of three marine bacteria showed 196 (or 55%) conserved residues in the alpha subunit and 114 (or 35%) conserved residues in the beta subunit. The highest degree of homology between any two species was between the luciferases of X. luminescens and Vibrio harveyi with 84% identity in the alpha subunits and 59% identity in the beta subunits.

Phosphorylation and dephosphorylation of histone (V (H5): controlled condensation of avian erythrocyte chromatin. Appendix: Phosphorylation and dephosphorylation of histone H5. II. Circular dichroic studies.

During avian erythropoiesis, the blast cells of the bone marrow mature into polychromatic erythrocytes (late stages knwon as reticulocytes) and then into mature red blood cells. When chickens are made anemic, the proportion of immature cells in the anemic bone marrow increases dramatically. The level of the lysine-rich histones. H1 and H5, has been found to be constant in the blood and bone marrow of normal and anemic chickens. This implies that H5 replaces H1 quantitatively. Urea-aluminum-lactate starch gel electrophoresis of H5 from these sources show that the degree of phosphorylation of H5 is proportional to the number of immature cells. About 70% of the H5 from the most immature bone marrow is phosphorylated, while 50% of the H5 from anemic blood is phosphorylated and H5 in normal blood is almost completely devoid of phosphate. When immature cells of the anemia bone marrow are incubated in the presence of inorganic 32P and [3H]lysine and [3H]arginine, extensive 32P incorporation is found in the phospho species. A minimum of nine phosphorylated components have been demonstrated by starch gel electrophoresis. The incorporation of 3H is time dependent. After 1.5 h of labeling, 3H is found in H5 containing 0, 1, 2, and 3 phosphates. tthe combined data suggest that newly synthesized H5 becomes progressively phosphorylated and that at the terminal stage of development, the phosphorylated H5 is completely dephosphorylated. These events may be important in controlling the timing of chromatin condensation.