Association of betaine-homocysteine S-methyltransferase with microtubules

C. Sandu, P. Nick, D. Hess, E. Schiltz, T. A. Garrow, R. Brandsch

Research output: Contribution to journalArticle

Abstract

In mammals, betaine of the mitochondrial matrix is used in the cytosol by betaine-homocysteine S-methyltransferase for methionine synthesis. The resulting dimethylglycine is shuttled back into the mitochondrial matrix for further degradation. Nanospray tandem mass spectrometry and N-terminal amino acid sequencing of microtubule-associated proteins from rat liver tubulin revealed that betaine-homocysteine S-methyltransferase is microtubule associated. This was confirmed by confocal laser scanning microscopy of HepG2 cells labeled with betaine-homocysteine S-methyltransferase-and α-tubulin-specific monoclonal antibodies. The association of betaine-homocysteine S-methyltransferase with the cytoskeleton may functionally integrate the mitochondrial and cytoplasmic compartments of choline degradation.

Original languageEnglish (US)
Pages (from-to)619-622
Number of pages4
JournalBiological Chemistry
Volume381
Issue number7
DOIs
StatePublished - Jan 1 2000

Keywords

  • Choline
  • Cytoskeleton
  • Mitochondria
  • Tubulin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry

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  • Cite this

    Sandu, C., Nick, P., Hess, D., Schiltz, E., Garrow, T. A., & Brandsch, R. (2000). Association of betaine-homocysteine S-methyltransferase with microtubules. Biological Chemistry, 381(7), 619-622. https://doi.org/10.1515/BC.2000.080