Characterization of an inhibitor of ribonucleic acid polymerase from the mycelial phase of Histoplasma capsulatum

Abstract

An inhibitor of ribonucleic acid polymerases has been obtained from the mycelial phase of Histoplasma capsulatum and partially characterized. The inhibitor, called histin, was purified 200-fold by heat treatment at 100 C and electrophoresis on polyacrylamide gels. Histin moved in electrophoresis as if negatively charged; it was insensitive to treatment with ribonuclease of deoxyribonuclease but was completely digested by Pronase. Sucrose gradient centrifugation suggests a molecular weight of 24,000. The possibility of a regulatory role for histin in the life cycle of H. capsulatum is discussed.