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Nucleic Acids Research, 1995, Vol. 23, No. 21 4426-4433
© 1995

Articles

Three subunits of the RNA polymerase II mediator complex are involved in glucose repression

Darius Balciunas and Hans Ronne*

Ludin Institute for Cancer Research, Uppsala Branch, Uppsala Biomedical Center Box 595, S-751 24 Uppsala, Swedan

*To whom correspondence should be addressed

Received July 5, 1995. Accepted October 4, 1995.

We have purified to homogeneity a DNase from a Crithidia fasciculata crude mitochondrlal lysate. The enzyme is present in two forms, either as a 32 kDa polypeptide or as a murtimer containing the 32 kDa polypeptide In association with a 56 kDa polypeptide. Native molecular weight measurements indicate that these forms are a monomer and possibly an {alpha}2ß2 tetramer, respectively. The monomeric and murtimeric forms of the enzyme are similar In their catalytic activities. Both digest double-stranded DNA about twice as efficiently as single-stranded DNA. They introduce single-strand breaks Into a supercoiled plasmid but do not efficiently make double-strand breaks. They degrade a linearized plasmid more efficiently than a nicked plasmid. Both enzymes degrade a 5'–32P-labeled double-stranded oligonucleotlde to completion, with the 5'–terminal nucleotide ultimately being released as a 5'– mononucleotide. One difference between the monomeric and murtimeric forms of the enzyme, demonstrated by a band shift assay, is that the murtimeric form binds tightly to double-stranded DNA, possibly aggregating it.


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