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Dihydroxyacetone synthase is localized in the peroxisomal matrix of methanol-grown Hansenula polymorpha

The subcellular localization of dihydroxyacetone synthase (DHAS) in the methylotrophic yeast Hansenula polymorpha was studied by various biochemical and immunocytochemical methods. After cell fractionation involving differential and sucrose gradient centrifugation of protoplast homogenates prepared from methanol-grown cells, DHAS cosedimented with the peroxisomal enzymes alcohol oxidase and catalase. Electron microscopy of this fraction showed that it contained mainly intact peroxisomes, whereas SDS-polyacrylamide gel electrophoresis revealed two major protein bands (75 and 78 kDa) which were identified as alcohol oxidase and DHAS, respectively. The localization of DHAS in peroxisomes was further established by immunocytochemistry. After immuno-gold staining carried out on ultrathin sections of methanol-grown H. polymorpha using DHAS-specific antibodies, labelling was confined to the peroxisomal matrix.

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MES:

2-(N-morpholino)ethanesulfonic acid

DTT:

dithiothreitol

SDS:

sodium dodecyl sulphate

TPP:

thiamin pyrophosphate

DHAS:

dihydroxyacetone synthase

GSH:

reduced glutathione

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1. Department of Micrbiology, University of Groningen, Biological Centre, Kerklaan 30, NL-9751 NN, Haren, The Netherlands

   Anneke C. Douma, Wim de Koning & Wim Harder

2. Laboratory of Electron Microscopy, University of Groningen, Biological Centre, Kerklaan 30, NL-9751 NN, Haren, The Netherlands

   Marten Veenhuis & Melchior Evers

1. Anneke C. Douma
2. Marten Veenhuis
3. Wim de Koning
4. Melchior Evers
5. Wim Harder

Douma, A.C., Veenhuis, M., de Koning, W. et al. Dihydroxyacetone synthase is localized in the peroxisomal matrix of methanol-grown Hansenula polymorpha . Arch. Microbiol. 143, 237–243 (1985). https://doi.org/10.1007/BF00411242

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• Received: 07 August 1985

• Accepted: 26 August 1985

• Issue Date: December 1985

• DOI: https://doi.org/10.1007/BF00411242

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