Localization of carnitine acetyltransferase in peroxisomes and in mitochondria of <i>n</i>‐alkane‐grown <i>candida tropicalis</i>

Kawamoto, Susumu; Ueda, Mitsuyoshi; Nozaki, Chikateru; Yamamura, Midori; Tanaka, Atsuo; Fukui, Saburô

doi:10.1016/0014-5793(78)81057-6

Cited by 55 publications

(20 citation statements)

References 15 publications

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“…By analogy with the suggested role for Gpd in peroxisomes of mammalian cells and Candida tropicalis (47)(48)(49), S. cerevisiae Gpd1p may contribute to maintain a suitable level of NAD ϩ for ␤-oxidation of fatty acids, either by local glycerol production (which would require presence of the yeast glycerol-3-phosphatase Gpp1p or Gpp2p) or by being part of glycerol 3-phosphate shuttle for transfer of reducing equivalents from the peroxisome to the cytosol. Such a shuttle may provide an alternative to the previously suggested malate/oxaloacetate cycle (50) to ensure continued reoxidation of NADH produced by the intraperoxisomal ␤-oxidation.…”

Section: Gpd2p Is Distributed Between Cytosol and Mitochondria-mentioning

confidence: 99%

Distinct Intracellular Localization of Gpd1p and Gpd2p, the Two Yeast Isoforms of NAD+-dependent Glycerol-3-phosphate Dehydrogenase, Explains Their Different Contributions to Redox-driven Glycerol Production

Valadi

Granath

Gustafsson

et al. 2004

Journal of Biological Chemistry

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Duringanaerobiosis Saccharomyces cerevisiae strongly increases glycerol production to provide for non-respiratory oxidation of NADH to NAD ؉ . We here report that respiratory-deficient cells become strictly dependent on the Gpd2p isoform of the NAD ؉ -linked glycerol-3-phosphate dehydrogenase (Gpd). The growth inhibition of respiratory incompetent cox18⌬ cells lacking GPD2 is reversed by the addition of acetoin, an alternative sink for NADH oxidation. Growth is also restored by addition of lysine or glutamic acid/glutamine, the synthesis of which involves production of mitochondrial NADH. Lysine produced a stronger growth stimulating effect than glutamic acid consistent with an upregulated expression of the IDP3 gene for peroxisomal synthesis of the glutamate precursor ␣-ketoglutarate. Gpd2p is known to be a cytosolic protein but possesses a classical mitochondrial presequence, which we show is sufficient for mitochondrial targeting. A partial mitochondrial localization of Gpd2p will provide for establishment of intramitochondrial redox balance under non-respiratory conditions. Gpd1p, the other Gpd isoform, is partly cytosolic and partly peroxisomal and becomes more strictly peroxisomal in respiratory-deficient mutants. The different cellular distribution of Gpd1p and Gpd2p thus appears to be the main reason Gpd1p cannot substitute for Gpd2p in cox18⌬gpd2⌬ cells, despite similar kinetic characteristics of the two iso-enzymes.

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Section: Gpd2p Is Distributed Between Cytosol and Mitochondria-mentioning

confidence: 99%

Distinct Intracellular Localization of Gpd1p and Gpd2p, the Two Yeast Isoforms of NAD+-dependent Glycerol-3-phosphate Dehydrogenase, Explains Their Different Contributions to Redox-driven Glycerol Production

Valadi

Granath

Gustafsson

et al. 2004

Journal of Biological Chemistry

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“…In a previous paper [7], we have demonstrated that carnitine acetyltransferases induced in alkane-grown cells of Candida tropicalis are localized in peroxisomes and mitochondria and that both enzymes take an essential part in the transfer of acetyl units from peroxisomes to mitochondria for the complete operation of the glyoxylate cycle. These enzymes in both organelles were separated by DEAE-Sephacel column chromatography [8].…”

mentioning

confidence: 92%

Characterization of peroxisomal and mitochondrial carnitine acetyltransferases purified from alkane‐grown Candida tropicalis

Ueda

Tanaka

Fukui

1984

European Journal of Biochemistry

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Properties of peroxisomal and mitochondrial carnitine acetyltransferases purified from an alkane-grown yeast, Candida tropicalis, were compared each other. The molecular weight of both enzymes was estimated to be about 420000 by analytical ultracentrifugation and gel filtration chromatography with Sepharose 6B. However, each enzyme gave two subunits on the polyacrylamide slab gel electrophoresis in the presence of sodium dodecyl sulfate : the peroxisomal enzyme (64000 and 57000) and the mitochondrial enzyme (64000 and 52000). The subcellularly distinct enzymes gave a similar amino acid composition except for the contents of some amino acids : glycine, valine, glutamic acid and aspartic acid. Their isoelectric point was somewhat different: 5.11 for the peroxisomal enzyme and 5.22 for the mitochondrial enzyme. Both enzymes had the same amino-terminal residue (glutamic acid or glutamine) and the heat stability, and was indistinguishable immunochemically. These results suggest that peroxisomal and mitochondrial carnitine acetyltransferases of C. tropicalis cells may be products of the same nuclear gene. Differences in the molecular weight of the subunits of the enzymes would result from modification or processing of the common protein in the step of distribution to the respective organelles, that is, so-called posttranslational modification.Carnitine acetyltransferase, which catalyzes the reversible transfer of acetyl group between CoA and I -carnitine, has an important role in the metabolism of fatty acids in eukaryotic cells, because acetyl-CoA, a final product of j-oxidation of fatty acids, is not permeable through the various organelle membranes but acetylcarnitine is permeable through these membranes [l -41. This enzyme has been detected in peroxis o m a and microsomes as well as in mitochondria of mammalian cells, and isolated from pigeon breast muscle and rat liver mitochondria [I -61. However, there is no information about the molecular identity of peroxisomal and mitochondrial carnitine acetyltransferases isolated from the same cells.In this connection, a variety of interesting problems remain to be elucidated: whether or not peroxisomal and mitochondrial carnitine acetyltransferases are products encoded by the same gene; how these two enzymes are distributed into two subcellular compartment if they are the same gene products ; what relationships exist between these two enzymes and the biogenesis of organelles, especially peroxisomes and so on. To acquire useful information on these matters, it is necessary to compare the molecular properties of peroxisomal and mitochondrial carnitine acetyltransferases.In a previous paper [7], we have demonstrated that carnitine acetyltransferases induced in alkane-grown cells of Candida tropicalis are localized in peroxisomes and mitochondria and that both enzymes take an essential part in the transfer of acetyl units from peroxisomes to mitochondria for the complete operation of the glyoxylate cycle. These enzymes in both organelles were separated by DEAE-Sephacel column...

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“…This latter mechanism requires the presence of carnitine acetyltransferase in both peroxisomes and mitochondria. For Candida tropicalis and Saccharomyces cerevisiae it has been shown that both peroxisomes and mitochondria indeed contain CAT activity (Kawamoto et al, 1978b;Atomi et al, 1993). Two camitine acetyltransferases have been cloned from S.cerevisiae.…”

Section: Introductionmentioning

confidence: 99%

Peroxisomal and mitochondrial carnitine acetyltransferases of Saccharomyces cerevisiae are encoded by a single gene.

Elgersma¹,

Roermund²,

Wanders³

et al. 1995

The EMBO Journal

182

149

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Carnitine acetyltransferase (CAT) is present in mitochondria and peroxisomes of oleate‐grown Saccharomyces cerevisiae. Both proteins are encoded by the same gene, YCAT, which encodes a protein with a mitochondrial targeting signal (MTS) at the N‐terminus, and a peroxisomal targeting signal type 1 (PTS‐1) at the C‐terminus. Deletion of both motifs revealed the presence of an additional internal targeting sequence. Import of CAT via this internal signal was shown to be dependent on PAS10, a protein which is required for the import of PTS‐1 containing proteins. An interaction of PAS10 with this internal targeting signal was demonstrated using the yeast two‐hybrid technique. Expression of the YCAT gene behind a heterologous promoter resulted in loss of peroxisomal targeting, indicating that differential targeting is controlled at transcriptional or translational level. Determination of the 5′‐ends of YCAT mRNAs revealed that YCAT transcripts initiating after the first AUG were present in oleate‐grown cells. These transcripts were virtually absent in acetate‐ or glycerol‐grown cells. We propose that in response to oleate, shorter transcripts are produced from which the peroxisomal form of CAT is translated, resulting in a CAT protein without a MTS, which can be targeted to peroxisomes.

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Localization of carnitine acetyltransferase in peroxisomes and in mitochondria of n‐alkane‐grown candida tropicalis

Cited by 55 publications

References 15 publications

Distinct Intracellular Localization of Gpd1p and Gpd2p, the Two Yeast Isoforms of NAD+-dependent Glycerol-3-phosphate Dehydrogenase, Explains Their Different Contributions to Redox-driven Glycerol Production

Distinct Intracellular Localization of Gpd1p and Gpd2p, the Two Yeast Isoforms of NAD+-dependent Glycerol-3-phosphate Dehydrogenase, Explains Their Different Contributions to Redox-driven Glycerol Production

Characterization of peroxisomal and mitochondrial carnitine acetyltransferases purified from alkane‐grown Candida tropicalis

Peroxisomal and mitochondrial carnitine acetyltransferases of Saccharomyces cerevisiae are encoded by a single gene.

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