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 language | English (US) |
---|---|
Pages (from-to) | 619-622 |
Number of pages | 4 |
Journal | Biological Chemistry |
Volume | 381 |
Issue number | 7 |
DOIs | |
State | Published - 2000 |
Externally published | Yes |
Keywords
- Choline
- Cytoskeleton
- Mitochondria
- Tubulin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Clinical Biochemistry