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Sci Rep. 2017 Aug 16;7(1):8315. doi: 10.1038/s41598-017-08088-6.

Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation.

Author information

1
Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan. matsush5@cclm.med.kyushu-u.ac.jp.
2
Department of Biochemistry and Molecular Biology, and Center for Mitochondrial Science and Medicine, Michigan State University, East Lansing Michigan, 48824-1319, USA. matsush5@cclm.med.kyushu-u.ac.jp.
3
Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan.
4
Section of Pediatric Dentistry, Division of Oral Health, Growth and Development, Faculty of Dental Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan.
5
Department of Biochemistry and Molecular Biology, and Center for Mitochondrial Science and Medicine, Michigan State University, East Lansing Michigan, 48824-1319, USA. lskaguni@msu.edu.
6
Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan. kang@cclm.med.kyushu-u.ac.jp.

Abstract

ClpXP is the major protease in the mitochondrial matrix in eukaryotes, and is well conserved among species. ClpXP is composed of a proteolytic subunit, ClpP, and a chaperone-like subunit, ClpX. Although it has been proposed that ClpXP is required for the mitochondrial unfolded protein response, additional roles for ClpXP in mitochondrial biogenesis are unclear. Here, we found that Drosophila leucine-rich pentatricopeptide repeat domain-containing protein 1 (DmLRPPRC1) is a specific substrate of ClpXP. Depletion or introduction of catalytically inactive mutation of ClpP increases DmLRPPRC1 and causes non-uniform increases of mitochondrial mRNAs, accumulation of some unprocessed mitochondrial transcripts, and modest repression of mitochondrial translation in Drosophila Schneider S2 cells. Moreover, DmLRPPRC1 over-expression induces the phenotypes similar to those observed when ClpP is depleted. Taken together, ClpXP regulates mitochondrial gene expression by changing the protein level of DmLRPPRC1 in Drosophila Schneider S2 cells.

PMID:
28814717
PMCID:
PMC5559520
DOI:
10.1038/s41598-017-08088-6
[Indexed for MEDLINE]
Free PMC Article

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