A 31P NMR study of the internal pH of yeast peroxisomes

Nicolay, Klaas; Veenhuis, Marten; Douma, A.C.; Harder, W.

doi:10.1007/bf00492902

Cited by 113 publications

(73 citation statements)

References 13 publications

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“…Recent results (Dansen et al 2000) and older works (Nicolay et al 1987) agree that the peroxisome internal pH is different from the cytoplasmic one. This ATPasemaintained intraperoxisomal pH could contribute to the generation of a proton motive force , which could play a role in transports.…”

Section: Transport To the Peroxisomesmentioning

confidence: 62%

Catabolism of hydroxyacids and biotechnological production of lactones by Yarrowia lipolytica

Waché¹,

Aguedo²,

Nicaud

et al. 2003

Appl Microbiol Biotechnol

114

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The g-and d-lactones of less than 12 carbons constitute a group of compounds of great interest to the flavour industry. It is possible to produce some of these lactones through biotechnology. For instance, g-decalactone can be obtained by biotransformation of methyl ricinoleate. Among the organisms used for this bioproduction, Yarrowia lipolytica is a yeast of choice. It is well adapted to growth on hydrophobic substrates, thanks to its efficient and numerous lipases, cytochrome P450, acylCoA oxidases and its ability to produce biosurfactants. Furthermore, genetic tools have been developed for its study. This review deals with the production of lactones by Y. lipolytica with special emphasis on the biotransformation of methyl ricinoleate to g-decalactone. When appropriate, information from the lipid metabolism of other yeast species is presented.

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Section: Transport To the Peroxisomesmentioning

confidence: 62%

Catabolism of hydroxyacids and biotechnological production of lactones by Yarrowia lipolytica

Waché¹,

Aguedo²,

Nicaud

et al. 2003

Appl Microbiol Biotechnol

114

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“…The molecular mechanisms behind this phenomenon are unknown, but may be related to the energy status of the organelles. Nicolay et al (1987) showed that a pH-gradient exists across the microbody membrane of yeasts, which is most probably generated and maintained by a proton translocating ATPase ). Bellion and G o o d m a n (1987) showed that import and assemblage of alcohol oxidase in microbodies of C. boidinii is an energy-dependent process which is prevented by uncouplers.…”

Section: Discussionmentioning

confidence: 99%

Evidence for functional heterogeneity among microbodies in yeasts

et al. 1989

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“…Stimulation was not found, however, when the oxidase was assayed with oleoyl-CoA or palmitoyl-CoA as the substrate at a pH of 5.0 -8.0, or with lauroyl-CoA at a pH of 6.0 or above. Therefore, it is uncertain whether PXP-18 stimulates acyl-CoA oxidase activity in vivo, but it is of interest that the internal pH of yeast peroxisomes has been reported to be low [40]. Further studies are necessary to elucidate the physiological function of not only PXP-18 but also nsLTPs from plant and animal sources.…”

Section: Possible Role Of Pxp-18mentioning

confidence: 99%

A novel peroxisomal nonspecific lipid‐transfer protein from Candida tropicalis

Tan

Okazaki

Kubota

et al. 1990

European Journal of Biochemistry

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We have sequenced the nucleotides of the gene POX18 that encodes PXP-18, a major peroxisomal polypeptide inducible by oleic acid in the yeast Candida tropicalis. POX18 had a single open reading frame of 127 amino acids. Some 33% of the amino acid sequence of the predicted basic polypeptide (13805 Da), was identical to that of the nonspecific lipid-transfer protein (sterol carrier protein 2) from rat liver. PXP-18, purified to near homogeneity from isolated peroxisomes, had an amino-terminal sequence identical to that of the predicted polypeptide except for the initiator methionine, and had nonspecific lipid-transfer activity comparable to that of its mammalian equivalents. Unexpectedly, PXP-18 lacked the cysteine residue thought to be essential for the activity of this protein in mammals. RNA blot analysis showed that the POX18 gene was expressed exclusively in cells grown on oleic acid, suggesting that PXP-18 has a role in the /I-oxidation of long-chain fatty acids. PXP-18 modulated acylcoenzyme A oxidase activity at low pH.Peroxisomal proteins are synthesized on free polysomes and imported post-translationally into the organelle, but most of them have no cleavable targeting (topogenic) sequence at the amino-terminus (for review, see [l]). The targeting sequences of five peroxisomal proteins from higher eucaryotes have been found at the carboxy-terminus and shown to contain a tripeptide, Ser-Lys/His-Leu, at or near the end of the sequence [2 -41. We have cloned genes encoding peroxisomal proteins of the yeast Candida tropicalis [5] and sequenced three genes for the subunits (PXP-2, PXP-4 and PXP-5) of acylCoA oxidase isozymes [6, 71 and the gene for catalase (PXP-9) [8]. None of the polypeptides encoded by these genes has the Ser-Lys/His-Leu sequence in their carboxy-terminal regions. The targeting information of PXP-4, which has a molecular mass of 78554 Da, was found in various locations by both in vitro [9] and in vivo [lo] experiments. Thus, the entire protein molecule must be systematically analysed if the yeast peroxisomal targeting sequence is to be identified. Since a small protein is more convenient for this purpose, we chose a 16-kDa protein, PXP-18, which is encoded by the gene POX18 and induced markedly by oleic acid [5]. Its function is not known.

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A 31P NMR study of the internal pH of yeast peroxisomes

Cited by 113 publications

References 13 publications

Catabolism of hydroxyacids and biotechnological production of lactones by Yarrowia lipolytica

Catabolism of hydroxyacids and biotechnological production of lactones by Yarrowia lipolytica

Evidence for functional heterogeneity among microbodies in yeasts

A novel peroxisomal nonspecific lipid‐transfer protein from Candida tropicalis

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