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Crystallographic and Functional Analyses of J-Domain of JAC1 Essential for Chloroplast Photorelocation Movement in Arabidopsis thaliana
Author(s) -
Akira Takano,
Noriyuki Suetsugu,
Masamitsu Wada,
Daisuke Kohda
Publication year - 2010
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/pcq089
Subject(s) - chloroplast , arabidopsis thaliana , arabidopsis , biology , protein domain , photosynthesis , biophysics , chemistry , botany , genetics , gene , mutant
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.

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