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 language | English |
|---|---|
| Pages (from-to) | 1372-1376 |
| Number of pages | 5 |
| Journal | Plant and Cell Physiology |
| Volume | 51 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Aug 1 2010 |
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All Science Journal Classification (ASJC) codes
- Physiology
- Plant Science
- Cell Biology
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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 journal › Article
}
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
PY - 2010/8/1
Y1 - 2010/8/1
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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UR - http://www.scopus.com/inward/citedby.url?scp=77955976763&partnerID=8YFLogxK
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 -