Elucidation Of The Redox Network In Chloroplasts By Analysis Of Affinity Between Thioredoxin And The Target Proteins

DOI

Bibliographic Information

Other Title
  • チオレドキシンと標的タンパク質の親和性解析による葉緑体内還元力ネットワークの解明

Description

Thioredoxin occurs in all living cells, and regulates the function of various target proteins by way of the dithiol-disulfide exchange reaction. In many organisms, thioredoxin is involved in protection from the oxidative stress. In phototrophs, thioredoxin has essential regulatory roles that link photosynthesis reaction and other reactions in the chloroplasts. In chloroplasts of Arabidopsis thaliana, 10 thioredoxin isoforms were revealed from the genome analysis. These isoforms were supposed to have their own preference for the target proteins. We considered that the selectivity of the target proteins by each of isoforms will be explained in term of affinity between "thioredoxin" and "target". We then measured affinity between thioredoxin and the target using surface-Plasmon-resonance method. Thus interaction between chloroplast thioredoxin isoforms and target proteins, FBPase and PrxQ, were analyzed. We discuss the affinity of target protein to thioredoxin isoforms based on these interaction studies.

Journal

Details 詳細情報について

  • CRID
    1390001205632453248
  • NII Article ID
    130006994159
  • DOI
    10.14841/jspp.2009.0.0879.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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