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Molecular and Cellular Biology, May 1999, p. 3829-3841, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Isolation of a Mammalian Homologue of a Fission Yeast Differentiation Regulator

Hanako Yamamoto, Kappei Tsukahara, Yoshihide Kanaoka, Shigeki Jinno, and Hiroto Okayama*

Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Bunkyo-Ku, Tokyo 113-0033, Japan

Received 26 October 1998/Returned for modification 14 December 1998/Accepted 8 February 1999

In the fission yeast Schizosaccharomyces pombe the nrd1+ gene encoding an RNA binding protein negatively regulates the onset of differentiation. Its biological role is to block differentiation by repressing a subset of the Ste11-regulated genes essential for conjugation and meiosis until the cells reach a critical level of nutrient starvation. By using the phenotypic suppression of the S. pombe temperature-sensitive pat1 mutant that commits lethal haploid meiosis at the restrictive temperature, we have cloned ROD1, a functional homologue of nrd1+, from rat and human cDNA libraries. Like nrd1+, ROD1 encodes a protein with four repeats of typical RNA binding domains, though its amino acid homology to Nrd1 is limited. When expressed in the fission yeast, ROD1 behaves in a way that is functionally similar to nrd1+, being able to repress Ste11-regulated genes and to inhibit conjugation upon overexpression. ROD1 is predominantly expressed in hematopoietic cells or organs of adult and embryonic rat. Like nrd1+ for fission yeast differentiation, overexpressed ROD1 effectively blocks both 12-O-tetradecanoyl phorbol-13-acetate-induced megakaryocytic and sodium butyrate-induced erythroid differentiation of the K562 human leukemia cells without affecting their proliferative ability. These results suggest a role for ROD1 in differentiation control in mammalian cells. We discuss the possibility that a differentiation control system found in the fission yeast might well be conserved in more complex organisms, including mammals.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Bunkyo-Ku, Tokyo 113-0033, Japan. Phone: 81-3-5689-0876. Fax: 81-3-3815-1490. E-mail: okayama{at}m.u-tokyo.ac.jp.

Molecular and Cellular Biology, May 1999, p. 3829-3841, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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