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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1975-6-27
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pubmed:abstractText |
Three DNA-dependent RNA polymerases have been isolated and partially purified from trophozoites of Acanthamoeba castellanii. Separated by DEAE-Sephadex chromatography, they have been designated polymerases, I, IIa and IIB according to their alpha-amanitin sensitivity and kinetic properties. I is completely insensitive to alpha-amanitin. IIa and IIb are sensitive to low concentrations (0.1 mug/ml) of alpha-amanitin; however, in order to achieve 100% inhibition much higher concentrations (130 mug/ml) are needed. Both I and II (a or b) have rather broad ionic strength optima (0.06--0.10 M (NH4)2SO4). All three prefer denatured over native DNA (I, 4:1; II, 2:1). Polymerase I utilizes magnesium better than manganese as divalent cation whereas II prefers manganese. When Acanthamoeba is transferred to a medium lacking nutrients, the cells undergo a synchronous differentiation resulting in cyst formation. In general agreement with the decrease in the rate of synthesis of its product (rRNA), the amount of polymerase I decreases relative to the amanitin sensitive polymerase(s). However, the absolute amount of polymerase I does not change. Rather, the levels of the amanitin sensitive enzymes increase during the first 10 h of encystment. Since the overall RNA synthesis rate decreases, these results suggest that the transcription rate is not controlled by specific enzyme levels alone.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amanitins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil Nucleotides
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
383
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-77
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1122326-Amanitins,
pubmed-meshheading:1122326-Amoeba,
pubmed-meshheading:1122326-DNA,
pubmed-meshheading:1122326-DNA-Directed RNA Polymerases,
pubmed-meshheading:1122326-Magnesium,
pubmed-meshheading:1122326-Manganese,
pubmed-meshheading:1122326-Osmolar Concentration,
pubmed-meshheading:1122326-Protein Conformation,
pubmed-meshheading:1122326-Time Factors,
pubmed-meshheading:1122326-Uracil Nucleotides
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pubmed:year |
1975
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pubmed:articleTitle |
DNA-dependent RNA polymerases from Acanthamoeba castellanii: properties and levels of activity during encystment.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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