About Us

Mitochondria, which are intracellular energy factories, are organelles that are indispensable for eukaryotic cells, and their morphology forms and distributes a tubular network-like structure throughout the cytoplasm, and dynamically repeats division and fusion. Recent studies have revealed that such mitochondrial morphology is very strongly linked to our health. 

In the cell group, the mechanism of “how is the morphological change of mitochondria controlled?” And “what kind of physiological meaning is it?” Is clarified at the molecular level, and finally. I am aiming to understand its physiological function.

Keywords: mitochondria, signal transduction, mechanism analysis, virus, innate immunity

Research theme

Koshiba Koshiba Takumi

Analysis of mitochondrial physiology

  • Mechanism analysis of mitochondrial dynamics
  • Studies on antiviral immunity and mitochondrial physiology

Nagadome solid double
Nagatome Shigemi

Colloidal chemical study of systemic surfactants

  • Properties of molecular aggregates of surfactants of sterols

Selected publications

1). Yoshizumi, T. et al. (2017) RLR-mediated antiviral innate immunity requires oxidative phosphorylation activity. Sci. Rep., 7, 5379.

2). Yoshizumi, T. et al. (2014) Influenza A viral protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity. Nat. Commun. , 5, 4713.

3). Koshiba, T. et al. (2011) Mitochondrial membrane potential is required for MAVS-mediated antiviral signaling.  Sci. Signal. , 4, ra7.

4). Yasukawa, K. et al. (2009) Mitofusin 2 inhibits mitochondrial antiviral signaling. Sci. Signal. , 2, ra47.

5). Koshiba, T. et al. (2004) Structural basis of mitochondrial tethering by mitofusin complexes.  Science 305, 858-862.


Membrane damages under high pressure of human erythrocytes agglutinated by concanavalin A.
Yamaguchi T, Tajiri K, Murata K, Nagadome S.
Colloids Surf B Biointerfaces. 2014 116: 695-9.

research content

RNA produced in cells plays a role as an information molecule of protein and a functional molecule such as expression regulation and chemical reaction. In addition, these RNAs undergo various chemical modifications (RNA modifications), and their information is rewritten and their functions change.

Our research group is conducting research aimed at “controlling” while “understanding” the intracellular RNA modification mechanism using chemical methods. Through these studies, we aim to understand living systems at the molecular level and at the same time develop molecular technologies that are useful to society.

Keywords: RNA editing, functional RNA, molecular design, gene mutation introduction, evolutionary molecular engineering

Research theme

Fukuda Hatatora
Fukuda Masatora

Understanding the molecular mechanism of RNA modification mechanism and development of control technology

  • Elucidation of physiological function and molecular mechanism of intracellular RNA editing mechanism
  • Elucidation of the target recognition mechanism of the editing enzyme ADAR
  • Development of site-specific RNA mutation introduction method using RNA editing mechanism
  • Construction of ADAR inhibitors by compound screening

Construction of artificial functional RNA aimed at controlling target gene expression

  • Design and functional evaluation of artificial ribozymes that recognize and cleave chemical modifications of target RNA
  • Construction of functional RNA that induces RNA modification at the target site

Selected publications

Construction of a guide-RNA for site-directed RNA mutagenesis utilizing intracellular A-to-I RNA editing.
Fukuda M, Umeno H, Nose K, Nishitarumizu A, Noguchi R, Nakagawa H.
Sci Rep. 2017 7:41478. Doi: 10.1038 / srep41478.

Identification of an RNA element for specific coordination of A-to-I RNA editing on HTR2C pre-mRNA.
Fukuda M, Oyama Y, Nishitarumizu A, Omura M, Nose K, Deshimaru M.
Genes Cells. 2015 20: 834-46. doi: 10.1111 / gtc.12272.

Improved design of hammerhead ribozyme for selective digestion of target RNA through recognition of site-specific adenosine-to-inosine RNA editing.
Fukuda M, Kurihara K, Yamaguchi S, Oyama Y, Deshimaru M.
RNA. 2014 20 (3): 392- 405. doi: 10.1261 / rna.041202.113.

Simultaneous detection of ATP and GTP by covalently linked fluorescent ribonucleotide sensors.
Nakano S, Fukuda M, Tamura T, Sakaguchi R, Nakata E, Morii T.
J Am Chem Soc. 2013 135 (9): 3465-73. Doi: 10.1021 / ja3097652.

A strategy for developing a hammerhead ribozyme for selective RNA cleavage depending on substitutional RNA editing.
Fukuda M, Kurihara K, Tanaka Y, Deshimaru M.
RNA. 2012 18 (9): 1735-44. Doi: 10.1261 / rna.033399.112.

research content

The “Protein Group” analyzes natural proteins purified from living organisms in the environment and recombinant proteins synthesized by genetic engineering with the power of chemistry, and examines the mechanism of life. In addition, new proteins may be created by artificially adding various functions. We are exploring the simple questions of life phenomena by clarifying the functions of the proteins that we have discovered, and are further expanding their applications to functional proteins and peptides.

Keywords: environmental factors, biological defense, protein synthesis, mutations, toxins

Research theme

Isao Kuraoka
Kuraoka Isao

Functional analysis of human DNA repair proteins and their regulatory mechanisms

  • Elucidation of biological defense system against DNA damage factors in the environment
  • Analysis of mutagenesis mechanism in vital function

Functional analysis of toxin proteins and their regulatory mechanisms

  • Elucidation of the biological defense system against poisonous organisms’ own poisons-
    How do poisonous organisms protect themselves from their own poisons? ~
  • Application of venomous snake protein as a drug discovery seed compound

Selected publications

Human endonuclease V is a ribonuclease specific for inosine-containing RNA.
Morita Y, Shibutani T, Nakanishi N, Nishikura K, Iwai S, Kuraoka I.
Nat Commun. 2013 4:2273. Doi: 10.1038 / ncomms3273.

XPG stabilizes TFIIH, allowing transactivation of nuclear receptors: implications for Cockayne syndrome in XP-G / CS patients.
Ito S, Kuraoka I, Chymkowitch P, Compe E, Takedachi A, Ishigami C, Coin F, Egly JM, Tanaka K.
Mol Cell. 2007 26 (2): 231-43.

Removal of oxygen free-radical-induced 5′, 8-purine cyclodeoxynucleosides from DNA by the nucleotide excision repair pathway in human cells.
Kuraoka I, Bender C, Romieu A, Cadet J, Wood RD, Lindahl T.
Proc Natl Acad Sci US A. 2000 97 (8): 3832-7.

Structural analysis and characterization of new small serum proteins from the serum of a venomous snake (Gloydius blomhoffii).
Shioi N, Deshimaru M, Terada S.
Biosci Biotechnol Biochem. 2014 78 (3): 410-9. Doi: 10.1080 / 09168451.2014. 890030.

Small serum protein-1 changes the susceptibility of an apoptosis-inducing metalloproteinase HV1 to a metalloproteinase inhibitor in habu snake (Trimeresurus flavoviridis).
Shioi N, Ogawa E, Mizukami Y, Abe S, Hayashi R, Terada S.
J Biochem. 2013 153 (1): 121-9. doi: 10.1093 / jb / mvs127.