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J Biol Chem, Vol. 273, Issue 51, 33889-33892, December 18, 1998
From the Department of Cell Biology, National Institute for Basic
Biology, Okazaki 444-8585, Japan
Autophagy is an intracellular process for bulk
degradation of cytoplasmic components. We recently found a protein
conjugation system essential for autophagy in the yeast,
Saccharomyces cerevisiae. The C-terminal
glycine of a novel modifier protein, Apg12p, is conjugated to a lysine
residue of Apg5p via an isopeptide bond. This conjugation reaction is
mediated by Apg7p, a ubiquitin activating enzyme (E1)-like enzyme, and
Apg10p, suggesting that it is a ubiquitination-like system
(Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T.,
George, M. D., Klionsky, D. J., Ohsumi, M., and Ohsumi, Y. (1998) Nature 395, 395-398). Although autophagy is a
ubiquitous process in eukaryotic cells, no molecule involved in
autophagy has yet been identified in higher eukaryotes. We reasoned
that this conjugation system could be conserved. Here we report cloning and characterization of the human homologue of Apg12 (hApg12). It is a
140-amino acid protein and possesses 27% identity and 48% similarity
with the yeast Apg12p, but no apparent homology to ubiquitin. Northern
blot analysis showed that its expression was ubiquitous in human
tissues. We found that it was covalently attached to another protein.
This target protein was identified to be the human Apg5 homologue
(hApg5). Mutagenic analyses suggested that this conjugation was formed
via an isopeptide bond between the C-terminal glycine of hApg12 and
Lys-130 of hApg5. These findings indicate that the Apg12 system is well
conserved and may function in autophagy also in human cells.
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