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Molecular and Cellular Biology, October 2000, p. 7784-7797, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mmf1p, a Novel Yeast Mitochondrial Protein Conserved throughout Evolution and Involved in Maintenance of the Mitochondrial Genome

Ellinor Oxelmark,1 Antonio Marchini,1 Ilaria Malanchi,1 Francesca Magherini,1 Laurence Jaquet,2 M. A. Nasser Hajibagheri,3 Kenneth J. Blight,3 Jean-Claude Jauniaux,2 and Massimo Tommasino1,*

Abteilung F02001 and F01002 (INSERM U375), Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany, and Imperial Cancer Research Fund, London, United Kingdom3

Received 24 February 2000/Returned for modification 28 March 2000/Accepted 12 July 2000

A novel protein family (p14.5, or YERO57c/YJGFc) highly conserved throughout evolution has recently been identified. The biological role of these proteins is not yet well characterized. Two members of the p14.5 family are present in the yeast Saccharomyces cerevisiae. In this study, we have characterized some of the biological functions of the two yeast proteins. Mmf1p is a mitochondrial matrix factor, and homologous Mmf1p factor (Hmf1p) copurifies with the soluble cytoplasmic fraction. Delta mmf1 cells lose mitochondrial DNA (mtDNA) and have a decreased growth rate, while Delta hmf1 cells do not display any visible phenotype. Furthermore, we demonstrate by genetic analysis that Mmf1p does not play a direct role in replication and segregation of the mtDNA. rho+ Delta mmf1 haploid cells can be obtained when tetrads are directly dissected on medium containing a nonfermentable carbon source. Our data also indicate that Mmf1p and Hmf1p have similar biological functions in different subcellular compartments. Hmf1p, when fused with the Mmf1p leader peptide, is transported into mitochondria and is able to functionally replace Mmf1p. Moreover, we show that homologous mammalian proteins are functionally related to Mmf1p. Human p14.5 localizes in yeast mitochondria and rescues the Delta mmf1-associated phenotypes. In addition, fractionation of rat liver mitochondria showed that rat p14.5, like Mmf1p, is a soluble protein of the matrix. Our study identifies a biological function for Mmf1p and furthermore indicates that this function is conserved between members of the p14.5 family.

* Corresponding author. Mailing address: Abteilung F0200, Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, D-69120 Heidelberg, Germany. Phone: 0049 6221 424945. Fax: 0049 6221 424932. E-mail: M.Tommasino{at}DKFZ-Heidelberg.de.

Molecular and Cellular Biology, October 2000, p. 7784-7797, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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