Evidence for the Bifunctional Nature of Mitochondrial Phosphatidylserine Decarboxylase: Role in Pdr3-Dependent Retrograde Regulation of <i>PDR5</i> Expression

Gulshan, Kailash; Schmidt, Jennifer A.; Shahi, Puja; Moye‐Rowley, W. Scott

doi:10.1128/mcb.00405-08

Cited by 43 publications

(65 citation statements)

References 60 publications

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“…1, B and C). Consistent with other studies (27), substitution of LGS for three alanines (LGS/AAA) completely prevented autocatalysis (Fig. 1B); furthermore, such a mutant failed to rescue the ethanolamine auxotrophy of the psd1⌬psd2⌬ strain (Fig.…”

Section: Characterization Of the Conserved Lgst Motif Of Psd1p-thesupporting

confidence: 78%

“…The ␤ subunit is integrated into the IM of the mitochondrion and serves to anchor the ␣ subunit to the intermembrane space (IMS) side of the IM (7,8). Although unrelated to Psd1p activity, the amino terminus of Psd1p is necessary and sufficient to induce multidrug resistance via Pdr5p signaling in yeast (27). Virtually nothing else is known about structural motifs required for Psd1p activity.…”

mentioning

confidence: 99%

“…In the yeast Saccharomyces cerevisiae, Psd1p lacking an NH 2 -terminal transmembrane domain is mislocalized to the matrix but still undergoes autocatalysis (7). Interestingly, although this mutant Psd1p allele retains catalytic activity in vitro (7), it is non-functional in vivo (7,27,31). This was taken as evidence that for Psd1p to function in vivo, it must be properly integrated into the IM with its active site facing the IMS (7).…”

mentioning

confidence: 99%

“…Autocatalytic processing of Psd1p, an obligate step for its function (25), can occur before or after its integration into the mitochondrial inner membrane (IM) (7). Autocatalysis occurs within a conserved LGST motif between the glycine and the serine residues through a process of serinolysis (7,(25)(26)(27)(28)(29). Serinolysis separates the enzyme into mature ␣ and ␤ subunits, which remain non-covalently associated, and generates a pyruvoyl prosthetic group at the NH 2 terminus of the ␣ subunit that is absolutely required for enzymatic activity (25,29,30).…”

mentioning

confidence: 99%

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Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Onguka¹,

Calzada²,

Ogunbona³

et al. 2015

Journal of Biological Chemistry

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Background: Autocatalytic processing is required for Psd1p function. Molecular requirements for Psd1p autocatalysis are largely undefined. Results: Psd1p autocatalysis occurs in yeast mutants lacking its substrate or mitochondrial-specific lipids. Furthermore, Psd1p re-directed to the endoplasmic reticulum undergoes autocatalysis and is functional in vivo. Conclusion: Psd1p autocatalysis does not require its substrate or mitochondrial-specific lipids, proteins, or co-factors. Significance: Once membrane-embedded, Psd1p is autocatalytically self-sufficient.

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Section: Characterization Of the Conserved Lgst Motif Of Psd1p-thesupporting

confidence: 78%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Onguka¹,

Calzada²,

Ogunbona³

et al. 2015

Journal of Biological Chemistry

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“…The sequence is not only required for the mitochondrial targeting but also for the correct processing into ␤ and ␣ fragments (33). Previously, plant PSD sequences from tomato and Arabidopsis were identified and expressed in the yeast psd1psd2 double mutant strain (10).…”

Section: N-terminal Deletion Of Pkpsd Yields Active Forms Of Enzyme-mentioning

confidence: 99%

Identification of Gene Encoding Plasmodium knowlesi Phosphatidylserine Decarboxylase by Genetic Complementation in Yeast and Characterization of in Vitro Maturation of Encoded Enzyme

Choi

Augagneur

Mamoun

et al. 2012

Journal of Biological Chemistry

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Background: Functional screening of malaria (P. falciparum) genes is a problem because of A ϩ T content. Results: Use of a P. knowlesi cDNA library and a yeast mutant identifies an important parasite cDNA/gene and reveals new regulation of lipid synthesis. Conclusion:The P. knowlesi library will enable extrapolation to P. falciparum. Significance: Functional screening of malaria genes is now greatly enhanced.

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Phosphatidylserine decarboxylases, key enzymes of lipid metabolism

Schuiki

Daum

2009

IUBMB Life

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SummaryPhosphatidylserine decarboxylases (PSDs) (E.C. 4.1.1.65) are enzymes which catalyze the formation of phosphatidylethanolamine (PtdEtn) by decarboxylation of phosphatidylserine (PtdSer). This enzymatic activity has been identified in both prokaryotic and eukaryotic organisms. PSDs occur as two types of proteins depending on their localization and the sequence of a conserved motif. Type I PSDs include enzymes of eukaryotic mitochondria and bacterial origin which contain the amino acid sequence LGST as a characteristic motif. Type II PSDs are found in the endomembrane system of eukaryotes and contain a typical GGST motif. These characteristic motifs are considered as autocatalytic cleavage sites where proenzymes are split into a-and b-subunits. The S-residue set free by this cleavage serves as an attachment site of a pyruvoyl group which is required for the activity of the enzymes. Moreover, PSDs harbor characteristic binding sites for the substrate PtdSer. Substrate supply to eukaryotic PSDs requires lipid transport because PtdSer synthesis and decarboxylation are spatially separated. Targeting of PSDs to their proper locations requires additional intramolecular domains. Mitochondrially localized type I PSDs are directed to the inner mitochondrial membrane by N-terminal targeting sequences. Type II PSDs also contain sequences in their N-terminal extensions which might be required for subcellular targeting. Lack of PSDs causes various defects in different cell types. The physiological relevance of these findings and the central role of PSDs in lipid metabolism will be discussed in this review.

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Evidence for the Bifunctional Nature of Mitochondrial Phosphatidylserine Decarboxylase: Role in Pdr3-Dependent Retrograde Regulation of PDR5 Expression

Abstract: Multidrug resistance in the yeast

Cited by 43 publications

References 60 publications

Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Identification of Gene Encoding Plasmodium knowlesi Phosphatidylserine Decarboxylase by Genetic Complementation in Yeast and Characterization of in Vitro Maturation of Encoded Enzyme

Phosphatidylserine decarboxylases, key enzymes of lipid metabolism

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