Electrophoretic study of histones in the unicellular alga Olisthodiscus luteus

Basic proteins were prepared from isolated nuclei of the unicellular alga Olisthodiscus luteus. The ratio of DNA/RNA/basic protein for these nuclei was 1:0.17:1.1, respectively, and the amino acid composition of the basic protein was very similar to that of Euglena and calf histones. The Olisthodiscus basic proteins were separated into four major components by polyacrylamide gel electrophoresis in four gel systems: (1) low pH disc gels containing 2.5 M urea; (2) two-dimensional low pH-urea gels in which the second dimension contained 1% Triton X-100; (3) slab gels containing 0.1% sodium dodecyl sulfate (SDS); (4) two-dimensional gels combining systems (1) and (3). The presence of four rather than five major histone fractions was shown to be not merely the result of proteolytic degradation. Results from the urea-containing gels suggest that an H1-like histone is missing, while electrophoresis in the SDS-containing gels shows the presence of a component resembling H1. In view of recent reports documenting the presence of five major histones in lower eukaryotes as well as in higher organisms, the presence of only four histones in Olisthodiscus suggests that this primitive eukaryote is unusual in its histone complement.