TY - JOUR
T1 - Crystallographic and functional analyses of j-domain of JAC1 essential for chloroplast photorelocation movement in Arabidopsis thaliana
AU - Takano, Akira
AU - Suetsugu, Noriyuki
AU - Wada, Masamitsu
AU - Kohda, Daisuke
N1 - Funding Information:
This work was supported by the Ministry of Education, Culture, Sports, Science and Technology of Japan (Targeted Proteins Research Program to D. K. and A. T., No. 13139203, 13304061, 16107002, 17084006 and 20227001 to M. W., No. 20870030 to N. S.).
Funding Information:
We thank Dr Sam-Geun Kong for assistance with the protein purification and Dr Nobuo Maita for advice about structure refinement. The experiments at the Photon Factory (Tsukuba Japan) were approved as proposals 2007G208 and 2009G021. This work was partly performed in the Cooperative Research Project Program of the Medical Institute of Bioregulation, Kyushu University.
PY - 2010/8
Y1 - 2010/8
N2 - 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.
AB - 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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U2 - 10.1093/pcp/pcq089
DO - 10.1093/pcp/pcq089
M3 - Article
C2 - 20562448
AN - SCOPUS:77955976763
VL - 51
SP - 1372
EP - 1376
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
SN - 0032-0781
IS - 8
ER -