Biomolecular Characterization Team
This team is engaged in structural characterization of biological molecules and in development of methodology for analysis of them to elucidate biological phenomena. Proteins in particular cause the biological phenomena and have various biological activities. Investigation of protein structures helps us to elucidate a mechanism of the biological activities, regulation of the activities, or gene functions. We support biological researchers by developing equipment and analytical methods and managing them, or giving advice on methodologies. A qualitative identification of small amount of proteins becomes easy with the development of the mass spectrometry, the excellent database, and the search program of it. The structural analysis and quantitative analysis of proteins with unknown modification or sequence is, however, still difficult. We are wrestling with development of new characterization methods for such proteins by combining sophisticated mass spectrometry with chemical methods. Our activities include mass spectrometry, protein chemical analyses, ultracentrifugal analysis, and x-ray analysis. We also established mail-in system with RIKEN SPring-8 center to deliver protein crystals prepared in Wako campus.
- Development and application of analytical methods for structural details on biological molecules
- Development of quantitative analysis of biomolecules
- Studies on structural biology and its related technologies
- RNA mass spectrometry
- Octorber 06,2010
- First-ever system for automatic protein hydrolysis developed using solid acid catalyst
- April 16, 2007
- Bioarchitect Research Group and Biomolecular Characterization Team in DRI produced contractile myofiber cells from myofibroblast by making use of intracellular stress.
- Masuda A, Dohmae N.:
"Automated Protein Hydrolysis Delivering Sample to a Solid Acid Catalyst for Amino Acid Analysis."
Anal Chem. , 82(21), 8939-45(2010) - Nakayama H, Akiyama M, Taoka M, Yamauchi Y, Nobe Y, Ishikawa H, Takahashi N, Isobe T.:
"Ariadne: a database search engine for identification and chemical analysis of RNA using tandem mass spectrometry data"
Nucleic Acids Res., 37(6): e47 (2009) - Tsukazaki T, Mori H, Fukai S, Ishitani R, Mori T, Dohmae N, Perederina A, Sugita Y, Vassylyev DG, Ito K, Nureki O.:
"Conformational transition of Sec machinery inferred from bacterial SecYE structures."
Nature, 455(7215):988-91 (2008) - Kawatani M, Okumura H, Honda K, Kanoh N, Muroi M, Dohmae N, Takami M, Kitagawa M, Futamura Y, Imoto M, Osada H.:
"The identification of an osteoclastogenesis inhibitor through the inhibition of glyoxalase I."
Proc. Natl. Acad. Sci. U. S. A., 105(33):11691-6 (2008) - Ito Y, Nakanomyo I, Motose H, Iwamoto K, Sawa S, Dohmae N, Fukuda H.:
"Dodeca-CLE peptides as suppressors of plant stem cell differentiation"
Science. 313(5788):842-5 (2006) - Kaku H, Nishizawa Y, Ishii-Minami N, Akimoto-Tomiyama C, Dohmae N, Takio K, Minami E, Shibuya N.:
"Plant cells recognize chitin fragments for defense signaling through a novel plasma membrane receptor"
Proc. Natl. Acad. Sci. U. S. A., 103(29):11086-91 (2006) - Kanai, Y, Dohmae, N, and Hirokawa, N
"Kinesin transports RNA: isolation and characterization of an RNA-transporting granule"
Neuron, 43(4), 513-25 (2004) - Umezu-Goto M, Kishi Y, Taira A, Hama K, Dohmae N, Takio K, Yamori T, Mills GB, Inoue K, Aoki J, Arai H.:
"Autotaxin has lysophospholipase D activity leading to tumor cell growth and motility by lysophosphatidic acid production."
J. Cell Biol., 158(2):227-33 (2002) - Fujiwara H, Hasegawa M, Dohmae N, Kawashima A, Masliah E, Goldberg MS, Shen J, Takio K, Iwatsubo T.:
"alpha-Synuclein is phosphorylated in synucleinopathy lesions"
Nat. Cell Biol., 4(2):160-4 (2002) - Masutani C, Kusumoto R, Yamada A, Dohmae N, Yokoi M, Yuasa M,Araki M, Iwai S, Takio K, Hanaoka F.:
"The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta"
Nature, 399(6737):700-4 (1999)

