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School Of Medicine
Life Sciences & Social Medicine
Department of Biochemistry
Introduction
Staff  
Yasuhiro HASHIMOTO (Professor)
Keirou SHIROTANI (Associate Professor)
KIyomitsu NARA (Research Assistant)
Satoshi FUTAKAWA (Research Assistant)
Yuriko TOOYAMA  
Kyoka HOSHI  
Ai KAMETAKA  
Research
1) Structure and function of branched-chain α-ketoacid dehydrogenase complex
  Branched-chain α-keto acid dehydrogenase complex (BCKADH) is one of the α-keto acid dehydrogenase complexes in mitochondria. Reactions catalyzed by the complex are rate-limiting step of branched-chain amino acids catabolism. BCKADH consists of E1, E2, and E3 as catalytic components. E2 component is formed by 24 E2 subunits. The E2 subunit has three domains of lipoyl-bearing-, E1/E3-binding- and inner-core domain. The multidomain structure is essential for formation of BCKADH and sequential 5 catalytic reactions without releasing of intermediates from the catalytic components (active-site coupling). These domains are connected by two interdomain segments (linkers). Recently we reported the linkers affect affinity for E1and the active site coupling of the lipoyldomain by analysis of non-vertebrate BCKADH. To elucidate the relation between function and structure of E2 linkers, we have set about preparing deletion mutants of chicken E2.
2) PCNP and NIRF
  We found a novel PEST-containing nuclear protein (PCNP). In general, PEST proteins are degraded rapidly, and play key roles in cellular functions such as transcriptional regulation and cell-cycle progression. To characterize PCNP, we sought PCNP-interacting factors and found NIRF (Np95/ICBP90-like RING finger) as a PCNP-binding partner. Experimentally, NIRF has been shown to function in cell-cycle regulation. Moreover, NIRF is predicted to be involved in some aspects of tumorigenesis. We hope to solve PCNP-NIRF interrelationship to get insights into human cancer progression and therapeutic intervention.
Education
We teach Biochemistry (Course and Practice) for 2nd and 3rd year students.
We also instruct Biochemical research training of 4th year student
Publications
Autoantibodies of sera from patients with primary biliary cirrhosis recognize the α subunit of the decarboxylase component of human branched-chain 2-oxo acid dehydrogenase complex.
Mori, T., Ono, K., Hakozaki, M., Kasukawa, R., and Kochi, H.
J. Hepatology, 34, 799-804 (2001)

cDNA cloning of chicken liver branched-chain α-keto acid dehydrogenase complex: Chicken specific residues of the acyltransferase affect of the overall activity and the interaction with the dehydrogenase.
Ono, K., Hakozaki, M., Suzuki, T., Mori, T., Hata, H. and Kochi, H.
European J Biochem. , 268, 727-736 (2001)

Characterization of rainbow trout branched-chain α-keto acid dehydrogenase complex: inter-domain segments of the E2 component affect the overall activity.
Hakozaki M., Ono K., Suzuki T., Hata H., Mori T., and Kochi H.
Comp Biochem Physiol. 132, 433-442 (2002)

NIRF, a novel RING finger protein, is involved in cell-cycle regulation.
Mori T., Li Y., Hata H., Ono K., and Kochi H.
Biochem Biophys Res Commun. 296, 530 (2002)
Detailed Information
 
To Contact Us
E-mail address: biochem1@fmu.ac.jp
 
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