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Journal of Biochemistry Advance Access published online on August 30, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm159
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© 2007 The Japanese Biochemical Society

Heme-regulated Degradation of {delta}-Aminolevulinate Synthase 1 in Rat Liver Mitochondria

Kazuhisa Yoshino1, Hiroshi Munakata2, Osamu Kuge1, Akio Ito1 and Tadashi Ogishima1,*

From the 1Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, 812-8581, and the 2Department of Biochemistry, School of Medicine, Kinki University, 377-2 Ohno-Higashi, Osaka-Sayama, 589-8511, Japan

*Address Correspondence to: Tadashi Ogishima, Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, 812-8581, Japan. Tel: +81-92-642-2601, Fax: +81-91-642-2607, E-mail: taogiscc{at}mbox.nc.kyushu-u.ac.jp

Received May 2, 2007; Accepted June 26, 2007


  Abstract

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 heme 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 heme, and suppressed by inhibition of heme biosynthesis. Furthermore, the heme-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 heme level and plays a crucial role in the regulation of heme biosynthesis.

Key Words: ALAS1, Heme and Metabolism, Metabolic regulation, Mitochondria, Protein degradation


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