Transcriptional regulation of the human mitochondrial peptide deformylase (PDF)

Biochemical and Biophysical Research Communications
Isabel Pereira-CastroLuisa Azevedo

Abstract

The last years of research have been particularly dynamic in establishing the importance of peptide deformylase (PDF), a protein of the N-terminal methionine excision (NME) pathway that removes formyl-methionine from mitochondrial-encoded proteins. The genomic sequence of the human PDF gene is shared with the COG8 gene, which encodes a component of the oligomeric golgi complex, a very unusual case in Eukaryotic genomes. Since PDF is crucial in maintaining mitochondrial function and given the atypical short distance between the end of COG8 coding sequence and the PDF initiation codon, we investigated whether the regulation of the human PDF is affected by the COG8 overlapping partner. Our data reveals that PDF has several transcription start sites, the most important of which only 18 bp from the initiation codon. Furthermore, luciferase-activation assays using differently-sized fragments defined a 97 bp minimal promoter region for human PDF, which is capable of very strong transcriptional activity. This fragment contains a potential Sp1 binding site highly conserved in mammalian species. We show that this binding site, whose mutation significantly reduces transcription activation, is a target for the Sp1 transcription factor, and...Continue Reading

References

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Sep 2, 2010·Molecular and Cellular Biology·Sindy Escobar-AlvarezDavid A Scheinberg

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Citations

Mar 31, 2016·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Jian GaoYouguang Zheng
Jun 28, 2019·Frontiers in Immunology·Patricia Martinez-QuinonesCamilla Ferreira Wenceslau

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