Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 41, Issue 5
Issue 237
Displaying 1-10 of 10 articles from this issue
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Perspective
Overview
  • Experimental Evidence for Information Redundancy in Amino Acid Sequences: Implication for Protein Folding and Evolution
    Satoshi AKANUMA, Yutaka KURODA
    Article type: scientific monograph
    Subject area: Infomation Science
    2001 Volume 41 Issue 5 Pages 224-229
    Published: 2001
    Released on J-STAGE: September 29, 2001
    DOIhttps://doi.org/10.2142/biophys.41.224
    JOURNAL FREE ACCESS
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    A protein three-dimensional structure is essentially determined by its amino acid sequence, and thus by the information contained therein. Although "protein folders" have long studied what physical forces are important to stabilize a protein structure, it is only recently that one has experimentally asked the question: how much and what information is prerequisite for stabilizing a protein structure. Here, we describe two recent experiments in which the information contents of two protein sequences have been dramatically decreased and nevertheless the proteins remain active and natively structured. We discuss the implication of these findings both from a protein structure and a molecular evolution point of view.
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  • The Interaction of ERM Proteins with Membranes and Adhesion Proteins: X-Ray Structural Studies of the Radixin FERM Domain
    Keisuke HAMADA, Toshio HAKOSHIMA
    Article type: scientific monograph
    Subject area: Infomation Science
    2001 Volume 41 Issue 5 Pages 230-234
    Published: 2001
    Released on J-STAGE: September 29, 2001
    DOIhttps://doi.org/10.2142/biophys.41.230
    JOURNAL FREE ACCESS
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    The N-terminal FERM domain of ERM (ezrin/radixin/moesin) proteins is responsible for membrane binding by interaction with phosphatidylinositol 4,5-bisphosphate (PIP2) and the adhesion proteins such as ICAMs. We have determined the crystal structures of the mouse radixin FERM domain, and its complexes with inositol-(1,4,5)-trisphosphate (IP3), which is a head group of PIP2, and with the ICAM-2 cytosolic tail. IP3 binds to a basic cleft between subdomains A and C, which is a different site from those found in PH domains. The ICAM-2 peptide binds to the subdomain C mediated by a β-β association and several side-chain interactions.
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Review
  • Structure and Function of DNA Replication Initiator Protein, RepE
    Hirofumi KOMORI, Chieko WADA, Kunio MIKI
    Article type: scientific monograph
    Subject area: Infomation Science
    2001 Volume 41 Issue 5 Pages 235-239
    Published: 2001
    Released on J-STAGE: September 29, 2001
    DOIhttps://doi.org/10.2142/biophys.41.235
    JOURNAL FREE ACCESS
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    The RepE initiator protein of F plasmid plays an essential role in initiating DNA replication in mini-F origin. RepE exhibits two major functions; the RepE monomer plays as a replication initiator which binds to direct repeats (iterons) in origin, while the RepE dimer as an autogenous repressor to the repE operator. The crystal structure of RepE monomer (RepE54) as a complex with an iteron DNA was determined as the first 3-D structure for procaryotic initiator proteins. The RepE monomer consists of topologically similar N- and C-terminal domains related by an internal pseudo two-fold symmetry, which has not been expected from its amino acid sequence. Both domains bind to two major grooves of iteron (19bp) with different binding affinities. The C-terminal domain plays the leading role in this binding, while the N-terminal domain has the additional role in dimerization.
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Topics
Experimental techniques
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