Inhibition of Histoplasma capsulatum ribonucleic acid polymerases by homologous and heterologous ribonucleic acid
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چکیده
منابع مشابه
Ribonucleic acid polymerases of the yeast phase of Histoplasma capsulatum.
Ribonucleic acid (RNA) polymerases of Histoplasma capsulatum (yeast phase) were fractionated by phosphocellulose chromatography and partially characterized. Three distinct, active fractions were seen. The major RNA polymerase species was inhibited strongly by alpha-amanitin, whereas the other two were resistant. When either slightly purified (HSE) extract or the major active component was assay...
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Two distinct ribonucleic acid polymerase activities were induced in HeLa cells by poxvirus infection. These activities differ both in their properties and the time of their appearance after infection. One catalyzes the dAT (copolymer of deoxyadenylate and deoxythymidylate)-primed conversion of adenosine triphosphate and uridine triphosphate into an acid-insoluble product. This enzyme is detecta...
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We compared the initiation specificities in vitro of deoxyribonucleic acid-dependent ribonucleic acid polymerases purified from two cyanobacteria, Fremyella diplosiphon and Anacystis nidulans, and from Escherichia coli. A restriction fragment made from lambda deoxyribonucleic acid was used as a template. The cyanobacterial and E. coli ribonucleic acid polymerases recognized the same lambda prom...
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Lomofungin, an antibiotic active against fungi, yeasts, and bacteria, was found to be a potent inhibitor of purified Escherichia coli deoxyribonucleic acid (DNA)-dependent ribonucleic acid (RNA) polymerase. It prevents RNA synthesis by a direct interaction with the polymerase and not with the template or substrate; chain elongation is halted promptly. Three DNA-dependent RNA polymerases isolate...
متن کاملCharacterization of an inhibitor of ribonucleic acid polymerase from the mycelial phase of Histoplasma capsulatum.
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...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1977
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.130.3.1387-1389.1977