Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 33, Issue 3
Displaying 1-11 of 11 articles from this issue
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  • [title in Japanese]
    [in Japanese]
    1993 Volume 33 Issue 3 Pages 129
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.129
    JOURNAL FREE ACCESS
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  • Crystal structures of DNA-binding proteins
    Toshio HAKOSHIMA
    1993 Volume 33 Issue 3 Pages 130-135
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.130
    JOURNAL FREE ACCESS
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    The structures of a variety of DNA-binding proteins reviel several classes of designs for recognition of a specific site on DNA. Three polymerases exhibit common features of their basic molecular architectures.
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  • Structures of DNA binding proteins and thir interaction with DNA
    Masahiro SHIRAKAWA
    1993 Volume 33 Issue 3 Pages 136-141
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.136
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    Structural studies of DNA binding proteins and their interaction with DNA by means of X-ray crystallography and nuclear magnetic resonance for the last decade have revealed the existence of some structural motifs for DNA binding proteins. Here is a brief review introducing the DNA binding motifs and their intraction with DNA.
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  • Structural Polymorphism of DNA and Its Recognizing-Proteins
    Yoshifumi NISHIMURA
    1993 Volume 33 Issue 3 Pages 142-147
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.142
    JOURNAL FREE ACCESS
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    A DNA molecule is not a simple featureless rod but it takes a characteristic conformation depending on its base sequence as well as on its molecular environment. Each feature is likely to be recognized by a specific protein. In principle, the DNA molecule exists as a double helical B form, which is a majour target of DNA-binding proteins. Even in the B form it can bend with or without proteins. In addition, various DNA structures including a single-standed stable mini-hairpin, double helical Z and A forms, a triple helix and a quadruple helix have been observed.
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  • Molecular communication between transcriptional activators and RNA polymerase
    Hiroji AIBA
    1993 Volume 33 Issue 3 Pages 148-153
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.148
    JOURNAL FREE ACCESS
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    The interation between transcriptional activator (s), and RNA polymerase plays a critical role in trancription activation. Several lines of evidence for the physical interaction between two proteins are summarized focusing on cAMP receptor protein (CRP). Recent progress of the study about the regions of both CRP and RNA polymerase which are involved in this interaction is discussed.
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  • Transcription Factors in Eukaryotes
    Masayoshi IMAGAWA
    1993 Volume 33 Issue 3 Pages 154-158
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.154
    JOURNAL FREE ACCESS
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    Many genes in eukaryotes are regulated at transcriptional level. Each gene has both general and specific cis-elements in its regulatory region. Transcription factors bind to these cis-elements and regulate the transcription activity. Phosphorylation plays an important role on these activation steps including nuclear translocation, DNA binding and protein-protein interactions. Some transcription factors make a family and homo-and hetero-dimer fomation modulates the complexed regulation.
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  • Transcriptional control by tbe CRE-binding protein, CRE-BP1
    Toshio MAEKAWA, Shunsuke ISHI
    1993 Volume 33 Issue 3 Pages 159-163
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.159
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    Two of the major classes of regulatory elements which contribute to transcriptional regulation by extracellular signals are the TRE and CRE sequence motifs. We have isolated the CRE-binding protein, CRE-BP1, which has a zinc finger structure as a transactivation domain located at the amino terminus and a leucine zipper motif found at the carboxy terminus. CRE-BP1 forms a heterodimer with jun family members and interestingly, the complex formation with CRE-BP1 changes c-jun from a TRE-binding protein to a CRE-binding protein. Finally it was also shown that CRE-BP1 mediated the EIA-induced transactivation.
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  • Signal transduction in vertebrate photoreceptors: light-dependent cGMP metabolism and its regulation mechanisms.
    Fumio HAYASHI
    1993 Volume 33 Issue 3 Pages 164-170
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.164
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    The outer segment of vertebrate photoreceptors is a sophisticated molecular device with remarkably high sensitivity and flexibility in photic signal reception and transduction. This device can detect single photons when dark-adapted and is also able to adapt to light intensities over a range of more than 6 log units. This device, is only a few picoliters in volume, contains a stack of discs on which 'the enzymatic machine', i.e. the cGMP-cascade translates the photic signal into cGMP breakdown. This eventually elicits closure of ion channels in the plasma membrane, consequent hyperpolarization of the membrane potential and also in the depletion of intracellular Ca2+. This Ca2+ depletion facilitates the recovery of cGMP not only by activating cGMP synthesis but also by desensitizing the cGMP-cascade. This article is a short review of recent findings on the mechanisms of the cGMP cascade and of the Ca2+ mediated regulaion of cGMP metabolism in vertebrate rod photoreceptors.
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  • Integration of protein functions into multi-action systems
    Atsushi IKAI
    1993 Volume 33 Issue 3 Pages 171-179
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.171
    JOURNAL FREE ACCESS
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    Life needs multifunctional machineries as sub-systems to carry out sets of biochemical reaction pathways. Examples are, mammalian fatty acid synthetase, an integrated system of seven active sites and an acyl carrier domain, and a giant serum protein named as α 2-macroglobulin or bet- ter known as a "molecular mouse trap". The former is a highly efficient molecular factory, and the latter represents the degree of sophistication of Rube Goldberg machine at the molecular level. In the case of fatty acid synthetase, integration of seven enzymes within the short reach of 4'-phosphopanthetein of acyl carrier domain imposes a new kinetic constraints on the system. α 2-macroglobulin comprises four sequential reaction steps in a "domino" style multi-action system, starting from its encounter with a proteinase. The proteinase then cleaves a peptide bond in the "bait region" sequence of α 2-macroglobulin, which triggers spontaneous hydrolysis of the "internal thiolester", which in turn causes a massive change in the quaternary structure of α 2-macroglobulin leading to entrapment of the proteinase within the molecular achitechture of α 2-macroglobulin and formation of recetor binding sites on its surface. Determination of the rate constants of each individual step in the above sequential process is our aim to understand the molecular mechanism of the transfer of structural information and its driving force within a multi-action protein system.
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  • [title in Japanese]
    [in Japanese], [in Japanese], [in Japanese], [in Japanese]
    1993 Volume 33 Issue 3 Pages 180-182
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.180
    JOURNAL FREE ACCESS
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  • Structural study on proteins by stopped-flow x-ray scattering.
    Hiroshi Kihara, Hirotsugu Tsuruta, Mamoru Sato, Atsushi Ikai, Kazumoto ...
    1993 Volume 33 Issue 3 Pages 183-186
    Published: May 25, 1993
    Released on J-STAGE: July 09, 2009
    DOIhttps://doi.org/10.2142/biophys.33.183
    JOURNAL FREE ACCESS
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