Proceedings of the Japan Academy, Series B

Reviews

Subaru studies of the cosmic dawn

Masanori IYE

2011 Volume 87 Issue 9 Pages 575-586
Published: November 11, 2011
Released on J-STAGE: November 11, 2011

DOIhttps://doi.org/10.2183/pjab.87.575

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An overview on the current status of the census of the early Universe population is given. Observational surveys of high redshift objects provide direct opportunities to study the early epoch of the Universe. The target population included are Lyman Alpha Emitters (LAE), Lyman Break Galaxies (LBG), gravitationally lensed galaxies, quasars and gamma-ray bursts (GRB). The basic properties of these objects and the methods used to study them are reviewed. The present paper highlights the fact that the Subaru Telescope group made significant contributions in this field of science to elucidate the epoch of the cosmic dawn and to improve the understanding of how and when infant galaxies evolve into mature ones.

(Communicated by Yoshihide KOZAI, M.J.A.)

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Molecular bases of thermophily in hyperthermophiles

Tadayuki IMANAKA

2011 Volume 87 Issue 9 Pages 587-602
Published: November 11, 2011
Released on J-STAGE: November 11, 2011

DOIhttps://doi.org/10.2183/pjab.87.587

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I reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakarensis KOD1 and its enzymes. The strain can grow at temperatures up to 100 °C, and also represents one of the simplest forms of life. As expected, all enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, I will focus on some enzymes whose three-dimensional structures are characteristic of thermostable enzymes. I will also add some examples on the stabilization of DNA, RNA, cytoplasmic membrane, and cytoplasmic solute.

(Communicated by Teruhiko Beppu, M.J.A.)

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Original Article

Flexible antibodies with nonprotein hinges

Daniel J. CAPON, Naoki KANEKO, Takayuki YOSHIMORI, Takashi SHIMADA, Fl ...

2011 Volume 87 Issue 9 Pages 603-616
Published: November 11, 2011
Released on J-STAGE: November 11, 2011

DOIhttps://doi.org/10.2183/pjab.87.603

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There is a significant need for antibodies that can bind targets with greater affinity. Here we describe a novel strategy employing chemical semisynthesis to produce symmetroadhesins: antibody-like molecules having nonprotein hinge regions that are more flexible and extendible and are capable of two-handed binding. Native chemical ligation was carried out under mild, non-denaturing conditions to join a ligand binding domain (Aβ peptide) to an IgG1 Fc dimer via discrete oxyethylene oligomers of various lengths. Two-handed Aβ–Fc fusion proteins were obtained in quantitative yield and shown by surface plasmon resonance to bind an anti-Aβ antibody with a K_D at least two orders of magnitude greater than the cognate Aβ peptide. MALDI-TOF MS analysis confirmed the protein/nonprotein/protein structure of the two-handed molecules, demonstrating its power to characterize complex protein-nonprotein hybrids by virtue of desorption/ionization mediated by peptide sequences contained therein. We anticipate many applications for symmetroadhesins that combine the target specificity of antibodies with the novel physical, chemical and biological properties of nonprotein hinges.

(Contributed by Koichi TANAKA, M.J.A.)

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