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Molecular and Cellular Biology, May 2001, p. 3589-3597, Vol. 21, No. 10
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.10.3589-3597.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Protein Interactions of the MLL PHD Fingers Modulate MLL Target Gene Regulation in Human Cells

Keri Fair,1 Melanie Anderson,1 Elena Bulanova,1 Huaifeng Mi,2 Maximilian Tropschug,2 and Manuel O. Diaz1,*

Cancer Center, Medical Center, Loyola University---Chicago, Maywood, Illinois 60153,1 and Institut für Biochemie und Molekularbiologie der Universität Freiburg, D-79104 Freiburg, Germany2

Received 29 June 2000/Returned for modification 29 August 2000/Accepted 15 February 2001

The PHD fingers of the human MLL and Drosophila trx proteins have strong amino acid sequence conservation but their function is unknown. We have determined that these fingers mediate homodimerization and binding of MLL to Cyp33, a nuclear cyclophilin. These two proteins interact in vitro and in vivo in mammalian cells and colocalize at specific nuclear subdomains. Overexpression of the Cyp33 protein in leukemia cells results in altered expression of HOX genes that are targets for regulation by MLL. These alterations are suppressed by cyclosporine and are not observed in cell lines that express a mutant MLL protein without PHD fingers. These results suggest that binding of Cyp33 to MLL modulates its effects on the expression of target genes.

* Corresponding author. Mailing address: Loyola University Medical Center, Cancer Center Bldg. 112, Rm. 333, 2160 South First Ave., Maywood, IL 60153. Phone: (708) 327-3172. Fax: (708) 327-3342. E-mail: mdiaz2{at}lumc.edu.

Molecular and Cellular Biology, May 2001, p. 3589-3597, Vol. 21, No. 10
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.10.3589-3597.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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