Haeme-regulated degradation of δ-aminolevulinate synthase 1 in rat liver mitochondria

Kazuhisa Yoshino, Hiroshi Munakata, Osamu Kuge, Akio Ito, Tadashi Ogishima

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


Protein turnover, which occurs at various rates, is critical for the homeostasis of cellular protein levels. However, the proteolysis systems that determine the turnover rate of mitochondrial proteins are largely unknown. Delta-aminolevulinic acid synthase (ALAS) 1, a rate-limiting enzyme in the haeme biosynthesis, is one of the mitochondrial proteins that have a very short lifetime. In this study, to reveal the regulatory mechanisms for ALAS1 degradation, we examined the turnover rates of ALAS1 in rat liver under several conditions. In primary rat hepatocytes, the degradation of ALAS1 was stimulated by haeme, and suppressed by inhibition of haeme biosynthesis. Furthermore, the haeme-stimulated degradation of ALAS1 was observed in the isolated mitochondria. These results suggested that, in mitochondria, there exists an ALAS1 degradation system that is regulated by cellular haeme level and plays a crucial role in the regulation of haeme biosynthesis.

Original languageEnglish
Pages (from-to)453-458
Number of pages6
JournalJournal of biochemistry
Issue number4
Publication statusPublished - Oct 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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