Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
Volume 1863, Issue 10, Pages 1331-1344Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbalip.2018.06.019
Keywords
Cardiolipin synthase; Yeast; Mitochondria; Schizosaccharomyces pombe; Phospholipid; Splicing
Funding
- Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of the Slovak Republic
- Slovak Academy of Sciences [2/0111/15, 1/0052/16, SAS-MOST JRP 2016/4]
- Slovak Research and Development Agency [APVV-15-0654]
- OPRaD - ERDF [ITMS 26240120027]
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Cardiolipin (CL) is a unique lipid component of mitochondria in all eukaryotes. It is important for the architecture of mitochondrial membranes and for mitochondrial dynamics. CL also creates a highly specific micro environment of mitochondrial protein machineries. CL biosynthetic pathway is, however, only partially characterized in the fission yeast Schizosaccharomyces pombe. Here we show that CL synthase is an essential protein in S. pombe. It is encoded by the ORE SPAC22A12.08c as a C terminal part of a tandem fusion protein together with a mitochondrial hydrolase of unknown function. Expression of S. pombe CL synthase is able to complement deletion of the CRD1 gene of Saccharomyces cerevisiae and, vice versa, S. cerevisiae CRD1 gene complements deletion of S. pombe SPAC22A12.08c. The proper expression of CL synthase and its partner in the tandem protein, the mitochondrial hydrolase, is regulated at the level of alternate intron splicing. The first part of the SPAC22A12.08c fusion protein could be translated from both major SPAC22A12.08c derived mRNAs, with and without intron IV. Functional CL synthase, however, is produced only from the minor SPAC22A12.08c derived mRNA that has intron IV retained. Thus, intron retention is a novel mechanism for the differential expression of two proteins that evolved as a fusion protein and are under the control of the same promoter.
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