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Life Sciences &
Social Medicine |
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Department of
Biochemistry |
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Introduction |
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Staff |
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Yasuhiro HASHIMOTO |
(Professor) |
Keirou SHIROTANI |
(Associate Professor) |
KIyomitsu NARA |
(Research Assistant) |
Satoshi FUTAKAWA |
(Research Assistant) |
Yuriko TOOYAMA |
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Kyoka HOSHI |
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Ai KAMETAKA |
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Research |
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1) |
Structure and function of branched-chain
α-ketoacid dehydrogenase complex |
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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 |
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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. |
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Education |
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We teach Biochemistry (Course and Practice)
for 2nd and 3rd year students.
We also instruct Biochemical research training
of 4th year student |
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Publications |
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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)
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Detailed Information |
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To Contact Us |
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E-mail address: biochem1@fmu.ac.jp |
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