Journal Article

Crystallographic and Functional Analyses of J-Domain of JAC1 Essential for Chloroplast Photorelocation Movement in <i>Arabidopsis thaliana</i>

Akira Takano, Noriyuki Suetsugu, Masamitsu Wada and Daisuke Kohda

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 51, issue 8, pages 1372-1376
Published in print August 2010 | ISSN: 0032-0781
Published online June 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq089
Crystallographic and Functional Analyses of J-Domain of JAC1 Essential for Chloroplast Photorelocation Movement in Arabidopsis thaliana

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  • Biochemistry
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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.

Keywords: Arabidopsis thaliana; chloroplast photorelocation; crystal structure; JAC1; J-domain

Journal Article.  2666 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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