Abstract
Purified yeast and mycelial phase rRNA from Histoplasma capsulatum was heat-formaldehyde deantured and analyzed by polyacrylamide gel electrophoresis. An average difference of 6.9% was seen in electrophoretic migration between the yeast and mycelial phase denatured 17 S rRNAs that was not apparent for the native 17 S rRNAs. This difference was statistically significant and could not be accounted for by random variation among gels electrophoresed in parallel. A significant difference was not found between the 25 S rRNAs of yeast and mycelial phase cells. Molecular weights of 1.28 × 10 6 for both the yeast and mycelial phase 25 S rRNA, and 0.79 × 10 6 and 0.73 × 10 6 for the yeast and mycelial phase 17 S rRNA, were estimated by using denaturing conditions which minimize conformational contributions to electrophoretic migration in polyacrylamide gels. In addition, we find that both the yeast and mycelial phase 17 S and 25 S rRNAs of H. capsulatum are smaller than their respective counterparts in S. cerevisiae. The results indicate that a structural difference may exist, at least between the 40 S subunits of H. capsulatum yeast and mycelial phase ribosomes.
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