Protein handling by molecular chaperones

2011 Fiscal Year Final Research Report

• Project Area: Protein community: organization and maintenance of protein functions
• Project/Area Number: 19058004
• Research Category: Grant-in-Aid for Scientific Research on Priority Areas
• Allocation Type: Single-year Grants
• Review Section: Biological Sciences
• Research Institution: Kyoto Sangyo University (2009-2011); Tokyo Institute of Technology (2007-2008)
• Principal Investigator: YOSHIDA Masasuke 京都産業大学, 総合生命科学部, 教授 (90049073)
• Co-Investigator(Kenkyū-buntansha): WATANABE Yohei 甲南大学, 理工学部, 講師 (40411839) ; MOTOJIMA Fumihiro 京都産業大学, 総合生命科学部, 助教 (70372464) ; NUREKI Satoshi 東京大学, 理学系研究科, 教授 (10272460)
• Project Period (FY): 2007 – 2011
• Keywords: シャペロン / シャペロニン / GroEL / DnaK / DafA / ClpB

Research Abstract

We found two kinds of new membrane chaperones. pspA repairs the leaks of ions through damaged membranes, and uncI assists membrane integration of hydrophobic c-subunit of ATP synthase. DnaK-DnaJ-DafA turns out to be inactive complex. As temperature raises, the complex dissociates and Dnak and DnaJ start to work as disaggregation chaperone in cooperation with ClpB. Polypeptide in the GroEL cage capped by GroES spends most time as tethered state. Then, it is released into the chaperonin cage or outside.

Research Products

• [Journal Article] Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding (2012)
  • Author(s): Motojima F, Motojima-Miyazaki Y, Yoshida M
  • Journal Title: Proc Natl Acad Sci USA Volume: 109(39) Pages: 15740-5
• [Journal Article] Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein (2012)
  • Author(s): Mizuno S, Nakazaki Y, Yoshida M, Watanabe YH
  • Journal Title: FEBS J Volume: 279 Pages: 1474-84. 663-6
  • DOI: doi:10.1111/j.1742-4658.2012.08540.x
  • Peer Reviewed
• [Journal Article] Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus (2011)
  • Author(s): Yamasaki T, Nakazaki Y, Yoshida M, Watanabe YH
  • Journal Title: FEBS J Volume: 278 Pages: 2395-403
  • DOI: doi:10.1111/j.1742-4658.2011.08167.x
  • Peer Reviewed
• [Journal Article] Yeast Prion Protein New1 Can Break Sup35 Amyloid Fibrils into Fragments in an ATP-dependent Manner (2011)
  • Author(s): InoueY, Kawai-Noma S, Koike-Takeshita A, Taguchi H, Yoshida M
  • Journal Title: Genes to Cell Volume: 16 Pages: 545-556
  • DOI: doi:10.1111/j.1365-2443.2011.01510.x
  • Peer Reviewed
• [Journal Article] Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside (2010)
  • Author(s): Motojima F, Yoshida M
  • Journal Title: EMBO J Volume: 29 Pages: 4008-19
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/20959808
  • Peer Reviewed
• [Journal Article] Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity (2010)
  • Author(s): Motojima-Miyazaki Y, Yoshida M, Motojima F
  • Journal Title: Biochem Biophys Res Commun Volume: 400 Pages: 241-5
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/20727857
  • Peer Reviewed
• [Journal Article] Temperature-dependent regulation of Thermus thermophilus DnaK/DnaJ chaperones by DafA protein (2009)
  • Author(s): Mizutani T, Nemoto S, Yoshida M, Watanabe YH
  • Journal Title: Genes Cells Volume: 14 Pages: 1405-13
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/19930469
  • Peer Reviewed
• [Journal Article] Probing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP (2009)
  • Author(s): Nojima T, Yoshida M
  • Journal Title: Biol Chem Volume: 284 Pages: 22834-9
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/19520865
  • Peer Reviewed
• [Journal Article] Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity (2009)
  • Author(s): Watanabe YH, Nakazaki Y, Suno R, Yoshida M
  • Journal Title: Biochem J Volume: 421 Pages: 71-7
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/19351326
  • Peer Reviewed
• [Journal Article] Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL (2008)
  • Author(s): Nojima T, Murayama S, Yoshida M, Motojima F
  • Journal Title: J. Biol. Chem Volume: 283 Pages: 18385-92
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/18430731
  • Peer Reviewed
• [Journal Article] Revisiting the GroEL-GroES reaction cycle via the symmetrical intermediate implied by novel aspects of the GroEL (D398A) mutant (2008)
  • Author(s): Koike-Takeshita A, Yoshida M, Taguchi H
  • Journal Title: J. Biol. Chem Volume: 283 Pages: 23774-81
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/18567584
  • Peer Reviewed
• [Journal Article] UncI protein can mediate ring-assembly of c-subunits of FoF1-ATP synthase in vitro (2008)
  • Author(s): Ozaki Y, Suzuki T, Kuruma Y, Ueda T, Yoshida M
  • Journal Title: Biochem Biophys Res Commun Volume: 67(3) Pages: 663-6
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/18182163
  • Peer Reviewed
• [Journal Article] The product of uncI gene in F1Fo-ATP synthase operon plays a chaperone-like role to assist c-ring assembly (2007)
  • Author(s): Suzuki T, Ozaki Y, Sone N, Feniouk BA, Yoshida M
  • Journal Title: Proc Natl Acad Sci USA Volume: 104(52) Pages: 20776-81
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/18083842
  • Peer Reviewed
• [Journal Article] Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes (2007)
  • Author(s): Kobayashi R, Suzuki T, Yoshida M
  • Journal Title: Mol Microbiol Volume: 66 Pages: 100-9
  • URL: http://www.ncbi.nlm.nih.gov/pubmed/18183492
  • Peer Reviewed
• [Presentation] "Football" with tethered polypeptide; renovation of chaperonin mechanism (2012)
  • Author(s): M. Yoshida, T. Ando, D. Yamamoto, F. Motojima
  • Organizer: EMBL symposium
  • Place of Presentation: Heiderburg, Germany
  • Year and Date: 2012-09-20
• [Presentation] Tethering mechanism of chaperonin (2011)
  • Author(s): Motojima F, Motojima-Miyazaki Y, Tanaka S, Yoshida M
  • Organizer: Cold Spring Harbor at Suzhou
  • Place of Presentation: China
  • Year and Date: 2011-09-27
• [Presentation] The folding pathway of blue fluorescent protein in spontaneous and chaperonin-assisted folding (2010)
  • Author(s): Motojima F, Yoshida M
  • Organizer: FASEB SRC, Protein folding in the cell
  • Place of Presentation: Saxtons River, Vermont. USA
  • Year and Date: 20100725-30
• [Presentation] Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside (2010)
  • Author(s): Motojima F, Yoshida M
  • Organizer: ISCP Nara
  • Place of Presentation: Nara, Japan
  • Year and Date: 2010-09-17
• [Presentation] Fold or escape; fates of substrate polypeptide in the critical GroEL/GroES intermediate (2010)
  • Author(s): Motojima F, Yoshida M
  • Organizer: Cold Spring Harbor Meeting
  • Place of Presentation: USA
  • Year and Date: 2010-05-04
• [Presentation] New Membrane Chaperones (2008)
  • Author(s): Kobayashi R, Ozaki Y, Suzuki T, Yoshida M
  • Organizer: Cold Spring Harbor Meeting
  • Place of Presentation: USA
  • Year and Date: 2008-05-02
• [Presentation] GroEL/ES-assisted folding of bfp starts from an extended state and is faster than free folding (2008)
  • Author(s): Motojima F, Yoshida M
  • Organizer: Cold Spring Harbor Meeting
  • Place of Presentation: USA
  • Year and Date: 2008-05-02
• [Remarks]
  • URL: http://www.cc.kyoto-su.ac.jp/~fmotojim/index-j.html