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Molecular and Cellular Biology, February 2006, p. 743-753, Vol. 26, No. 3
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.3.743-753.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Translational Regulation of Nuclear Gene COX4 Expression by Mitochondrial Content of Phosphatidylglycerol and Cardiolipin in Saccharomyces cerevisiae

Xuefeng Su and William Dowhan*

Department of Biochemistry and Molecular Biology, University of Texas Medical School, and Graduate School of Biomedical Sciences, Houston, Texas 77030

Received 9 June 2005/ Returned for modification 8 July 2005/ Accepted 1 November 2005

Previous results indicated that translation of four mitochondrion-encoded genes and one nucleus-encoded gene (COX4) is repressed in mutants (pgs1{Delta}) of Saccharomyces cerevisiae lacking phosphatidylglycerol and cardiolipin. COX4 translation was studied here using a mitochondrially targeted green fluorescence protein (mtGFP) fused to the COX4 promoter and its 5' and 3' untranslated regions (UTRs). Lack of mtGFP expression independent of carbon source and strain background was established to be at the translational level. The translational defect was not due to deficiency of mitochondrial respiratory function but was rather caused directly by the lack of phosphatidylglycerol and cardiolipin in mitochondrial membranes. Reintroduction of a functional PGS1 gene under control of the ADH1 promoter restored phosphatidylglycerol synthesis and expression of mtGFP. Deletion analysis of the 5' UTRCOX4 revealed the presence of a 50-nucleotide fragment with two stem-loops as a cis-element inhibiting COX4 translation. Binding of a protein factor(s) specifically to this sequence was observed with cytoplasm from pgs1{Delta} but not PGS1 cells. Using HIS3 and lacZ as reporters, extragenic spontaneous recessive mutations that allowed expression of His3p and ß-galactosidase were isolated, which appeared to be loss-of-function mutations, suggesting that the genes mutated may encode the trans factors that bind to the cis element in pgs1{Delta} cells.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, 6431 Fannin St., Suite 6.200, University of Texas—Houston Medical School, Houston, TX 77030. Phone: (713) 500-6100. Fax: (713) 500-0562. E-mail: william.dowhan{at}uth.tmc.edu.

Molecular and Cellular Biology, February 2006, p. 743-753, Vol. 26, No. 3
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.3.743-753.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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