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Nucleic Acids Research, 2002, Vol. 30, No. 9 1977-1984
© 2002 Oxford University Press

Purification and characterization of transcription factor IIIA from Acanthamoeba castellanii

Nicholas Polakowski and Marvin R. Paule*

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA

TFIIIA is required to activate RNA polymerase III transcription from 5S RNA genes. Although all known TFIIIA homologs harbor nine zinc fingers that mediate DNA binding, very limited sequence homology is found among these proteins, which reflects unique properties of some TFIIIA homologs. For example, the Acanthamoeba castellanii homolog directly regulates 5S RNA transcription. We have purified and characterized A.castellanii TFIIIA (AcTFIIIA) as a step toward obtaining a clearer understanding of these differences and of the regulatory process. AcTFIIIA is 59 kDa, significantly larger than all other TFIIIA homologs isolated to date. Nevertheless, it exhibits a DNase I footprint very similar to those produced by the smaller vertebrate TFIIIA homologs, but distinct from the smaller footprint of the 51 kDa TFIIIA from Saccharomyces cerevisiae. Similar footprinting is not reflected in greater sequence similarity between the A.castellanii and vertebrate promoters.

* To whom correspondence should be addressed. Tel: +1 970 491 6748; Fax: +1 970 491 0494; Email: mpaule{at}lamar.colostate.edu


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