Crystallographic and functional analyses of j-domain of JAC1 essential for chloroplast photorelocation movement in Arabidopsis thaliana

Akira Takano, Noriyuki Suetsugu, Masamitsu Wada, Daisuke Kohda

    Research output: Contribution to journalArticle

    10 Citations (Scopus)

    Abstract

    An auxilin-like J-domain-containing protein, JAC1, is necessary for chloroplast movement in Arabidopsis thaliana, to capture photosynthetic light efficiently under weak light conditions. Here, we performed crystallographic and functional analyses of the J-domain of JAC1. The crystal structure of the J-domain is quite similar to that of bovine auxilin, and possesses a similar positively charged surface, which probably forms the interface with the Hsp70 chaperone. The mutation of the highly conserved HPD motif of the JAC1 J-domain abrogated the chloroplast photorelocation response. These results suggest that the requirement of JAC1 in chloroplast photorelocation movement is attributable to the J-domain's cochaperone activity.

    Original languageEnglish
    Pages (from-to)1372-1376
    Number of pages5
    JournalPlant and Cell Physiology
    Volume51
    Issue number8
    DOIs
    Publication statusPublished - Aug 1 2010

    Fingerprint

    Auxilins
    Chloroplasts
    Arabidopsis
    Arabidopsis thaliana
    chloroplasts
    Light
    crystal structure
    mutation
    Mutation
    cattle
    proteins

    All Science Journal Classification (ASJC) codes

    • Plant Science
    • Physiology
    • Cell Biology

    Cite this

    Crystallographic and functional analyses of j-domain of JAC1 essential for chloroplast photorelocation movement in Arabidopsis thaliana. / Takano, Akira; Suetsugu, Noriyuki; Wada, Masamitsu; Kohda, Daisuke.

    In: Plant and Cell Physiology, Vol. 51, No. 8, 01.08.2010, p. 1372-1376.

    Research output: Contribution to journalArticle

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