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Molecular and Cellular Biology, January 1999, p. 796-806, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Histone Acetyltransferase and Protein Kinase Activities Copurify with a Putative Xenopus RNA Polymerase I Holoenzyme Self-Sufficient for Promoter-Dependent Transcription

Annie-Claude Albert, Michael Denton,dagger Milko Kermekchiev, and Craig S. Pikaard*

Biology Department, Washington University, St. Louis, Missouri 63130

Received 4 May 1998/Returned for modification 5 June 1998/Accepted 23 September 1998

Mounting evidence suggests that eukaryotic RNA polymerases preassociate with multiple transcription factors in the absence of DNA, forming RNA polymerase holoenzyme complexes. We have purified an apparent RNA polymerase I (Pol I) holoenzyme from Xenopus laevis cells by sequential chromatography on five columns: DEAE-Sepharose, Biorex 70, Sephacryl S300, Mono Q, and DNA-cellulose. Single fractions from every column programmed accurate promoter-dependent transcription. Upon gel filtration chromatography, the Pol I holoenzyme elutes at a position overlapping the peak of Blue Dextran, suggesting a molecular mass in the range of ~2 MDa. Consistent with its large mass, Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gels reveal approximately 55 proteins in fractions purified to near homogeneity. Western blotting shows that TATA-binding protein precisely copurifies with holoenzyme activity, whereas the abundant Pol I transactivator upstream binding factor does not. Also copurifying with the holoenzyme are casein kinase II and a histone acetyltransferase activity with a substrate preference for histone H3. These results extend to Pol I the suggestion that signal transduction and chromatin-modifying activities are associated with eukaryotic RNA polymerases.

* Corresponding author. Mailing address: Biology Department, Washington University, Campus Box 1137, One Brookings Dr., St. Louis, MO 63130. Phone: (314) 935-7569. Fax: (314) 935-4432. E-mail: pikaard{at}biodec.wustl.edu.

dagger Present address: Department of Biochemistry, Kansas State University, Manhattan, KS 66506.

Molecular and Cellular Biology, January 1999, p. 796-806, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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