Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein.

A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Abstract Text:

    takayuki k nemotoTakayuki K Nemoto,yutaka fukumaYutaka Fukuma,hideaki itohHideaki Itoh,takashi takagiTakashi Takagi,toshio onoToshio Ono,

    The 70-kDa heat shock protein (Hsp70) is predominantly present intracellularly as a monomer, but a small population is converted to dimers and oligomers under certain conditions. In the present study, we investigated the dimeric structure of human inducible Hsp70. As reported earlier, the C-terminal client-binding domain (amino acids 382-641) was required for the dimerization. A 40-amino acid deletion in the client-binding domain from either the N-terminus or C-terminus greatly enhanced the dimerization potential of Hsp70. Limited proteolysis indicated that the dimer formed through truncation from the C-terminus had a conformation similar to that of the non-truncated form. Truncation experiments demonstrated that the client-binding sub-domain (amino acids 382-520) with its adjacent region up to amino acid 541 was not sufficient for the dimerization but that the region up to amino acid 561 was sufficient. Interestingly, the dimer formed through truncation from the C-terminus acquired a homomeric disulfide bridge at Cys574.

    A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Publishing Authors By Initials

    tk nemotoTK Nemoto,y fukumaY Fukuma,h itohH Itoh,t takagiT Takagi,t onoT Ono,

    For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 139

    Page Numbers: 677-87

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Apr

    YEAR: 2006

    A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Keywords Mesh Terms:

    KEYWORDS: Recombinant Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein. Information

    Substance Name: Cysteine

    Registry Number: 52-90-4

    Grant and Affiliation Information for A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein.

    AFFILIATION: Division of Oral Molecular Biology, Department of Developmental and Reconstructive Medicine, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588. tnemoto@net.nagasaki-u.ac.jp

    Country: Japan

    Japan Research PublicationJapan Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Biochem

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News