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 journalArticlepeer-review

    13 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 2010

    All Science Journal Classification (ASJC) codes

    • Physiology
    • Plant Science
    • Cell Biology

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