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Researcher Information

last modified:2017/05/23

Associate Professor KANEMORI Masaaki

Mail

Faculty, Affiliation

Faculty of Natural System, Institute of Science and Engineering Functional Biochemistry

College and School Educational Field

Division of Natural Sciences, Graduate School of Natural Science and Technology
Division of Life Sciences, Graduate School of Natural Science and Technology
School of Natural System, College of Science and Engineering

Laboratory

 TEL:076-264-6229 FAX:076-264-6230

Academic Background

【Academic background(Doctoral/Master's Degree)】
Kyoto University Doctor 1994 Completed
【Academic background(Bachelor's Degree)】
Kyushu University 1988

Career

HSP Research Institute(1994/04/01-2000/03/17)

Year & Month of Birth

1965/09

Academic Society


Award

○grant from Yamada Science Foundation(2001/09/25)

Specialities

Functional biochemistry

Speciality Keywords

stress response, molecular chaperone, ATP-dependent protease

Research Themes

Substrate recognition mechanism of Hsp70 chaperone system

It has been thought that a polypeptide spontaneously folds into its functional state according to the primary amino acid sequence. However, most newly synthesized polypeptides require a set of molecular chaperones to fold their native conformations. Because cytosol is highly crowded with macromolecules, a newly synthesized polypeptide could improperly interact with them and fail to fold. Molecular chaperones protects newly synthesized polypeptides from improper interactions or aggregation, and assist them in maturing into proteins. Although Hsp70 is the major chaperone and has been studied for long time, its substrate-recognition mechanism is not perfectly understood. I have studied Hsp70 using techniques of molecular biology and biochemistry.

Books

Papers

  •  DnaJ-Promoted Binding of DnaK to Multiple Sites on σ32 in the Presence of ATP Aki Noguchi, Ayami Ikeda, Moeka Mezaki, Yoshihiro Fukumori, Masaaki Kanemori JOURNAL OF BACTERIOLOGY 196 9 1694-1703 2014/05
  •  Synergistic binding of DnaJ and DnaK chaperones to the heat shock transcriptionfactor s32 assures its characteristic high metabolic instability. Implications for heat shock protein 70 (Hsp70)-Hsp40 mode of function. Hirotaka Suzuki, Ayami Ikeda, Sachie Tsuchimoto, Ko-ichi Adachi, Aki Noguchi, Yoshihiro Fukumori, Masaaki Kanemori JOURNAL OF BIOLOGICAL CHEMISTRY 287 23 19275-19283 2012/06
  •  Conserved region 2.1 of Escherichia coli heat shock transcription factor s32 is required for modulating both metabolic stability and transcriptional activity JOURNAL OF BACTERIOLOGY 186 22 7474-7480 2004/11
  •  Dynamic interplay between antagonistic pathways controlling the s32 level in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 97 11 5860-5865 2000/05
  •  Marked instability of the s32 heat shock transcription factor at high temperature - implication for heat shock regulation. The Journal of Biological Chemistry 273 31 22002-22007 1999/07

show all

  •  Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Applied and Emvironmental Microbiology 66 3 884-889 2000/03
  •  The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli. JOURNAL OF BACTERIOLOGY 181 12 3674-3680 1999/06
  •  Heat-induced synthesis of s32 in Escherichia coli: structural and functional dissection of rpoH mRNA secondary structure. JOURNAL OF BACTERIOLOGY 181 2 401-410 1999/01
  •  Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Applied and Emvironmental Microbiology 64 5 1694-1699 1998/05
  •  Nitrate reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum MS-1: purification and sequence analyses. CANADIAN JOURNAL OF MICROBIOLOGY 49 3 197-206 2003/03
  •  Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of s32 and abnormal proteins in Escherichia coli. JOURNAL OF BACTERIOLOGY 179 23 7219-7225 1997/12
  •  Purification, characterization and sequence analyses of extracellular giant hemoglobin from Oligobrachia mashikoi Taro Nakagawa, Seiko Onoda, Masaaki Kanemori, Yuichi Sasayama, Yoshinori Fukumori ZOOLOGICAL SCIENCE 22 3 283-291 2005/03
  •  Identification of endosymbionts in Oligobrachia mashikoi (Siboglinidae, Annelida) Norihiro Kubota, Masaaki Kanemori, Yuichi Sasayama, Masato Aida, Yoshihiro Fukumori Microbes and Environments 22 2 136-144 2007/05
  •  Actual distribution of bacteriocytes in the trophosome of a beard worm (Oligobrachia mashikoi, Siboglinidae, Annelida): clarification using whole-mount in situ hybridization M. Deguchi, N. Kubota, A. Matsuno, M. Kanemori, Y. Fukumori, Y. Sasayama ACTA ZOOLOGICA 88 2 129-135 2007/04
  •  Direct evidence that extra-cellular giant hemoglobin is produced in chloragogen tissues in a beard worm, Oligobrachia mashikoi (Frenulata, Siboglinidae, Annelida) S. Nakahama, T. Nakagawa, M. Kanemori, Y. Fukumori, and Y. Sasayama Zoological Science 25 1247-1252 2008
  •  Distribution and population of free-living cells related to endosymbiont A harbored in Oligobrachia mashikoi (a Siboglinid Polychaete) M. Aida, M. Kanemori, N. Kubota, M. Matada, Y. Sasayama, and Y. Fukumori Microbes and Environments 23 1 81-88 2008
  •  GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. JOURNAL OF BIOLOGICAL CHEMISTRY 277 52 50621-50628 2002/12

Conference Presentations

Arts and Fieldwork

Patent

Theme to the desired joint research

Grant-in-Aid for Scientific Research

○「分子シャぺロンやATP依存性プロテアーゼにより認識されるσ32上の構造の同定」(2001-) 

Classes (Bachelors)

○Chemistry for Education(2017)
○Biochemistry 2(2017)
○Research Work in Biology(2)(2017)
○Research Seminar in Biology (2)(2017)
○Biochemistry Lab(2017)
○Guide to Biology and Earth Sciences(2017)
○Biology for Education(2017)
○Biochemistry 2(2017)
○Biology for Education(2017)
○Practical Seminar for Teaching Profession C / Junior High School・High School(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Research Work in Biology(1)(2017)
○Biology for Education(2017)
○Biochemistry 1(2017)
○Research Seminar in Biology (1)(2017)
○Internship(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2017)
○Molecular and Cellular Biology(2016)
○Molecular and Cellular Biology(2016)
○Molecular and Cellular Biology(2016)
○Biochemistry 1(2016)
○Biology for Education(2016)
○Biochemistry 2(2016)
○Biology for Education(2016)
○Biology for Education(2016)
○Practical Seminar for Teaching Profession C / Junior High School・High School(2016)
○Research Work in Biology(1)(2016)
○Research Work in Biology(2)(2016)
○Biochemistry Lab(2016)
○Research Seminar in Biology (1)(2016)
○Research Seminar in Biology (2)(2016)
○Guide to Biology and Earth Sciences(2016)

Classes (Graduate Schools)

○Systems structure and function in biomolecules B(2017)
○Topics in protein science(2017)
○Topics in protein science(2017)
○Topics in protein science(2017)
○Topics in protein science(2017)
○Basic Systems Biology A(2016)
○Research work in Systems Biology(2016)
○Exercise in Systems Biology 2B(2016)
○Exercise in Systems Biology 2A(2016)
○Exercise in Systems Biology 1B(2016)
○Exercise in Systems Biology 1A(2016)
○Basic Exercise in Systems Biology(2016)
○Research Skills B(2016)
○Research Skills A(2016)
○Systems structure and function in biomolecules B(2016)

International Project

International Students

Lecture themes

Others (Social Activities)

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