4.7 Article

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

期刊

PLANT AND CELL PHYSIOLOGY
卷 51, 期 8, 页码 1372-1376

出版社

OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcq089

关键词

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

资金

  1. Ministry of Education, Culture, Sports, Science and Technology of Japan [13139203, 13304061, 16107002, 17084006, 20227001, 20870030]
  2. Grants-in-Aid for Scientific Research [16107002, 13304061, 20870030, 20227001] Funding Source: KAKEN

向作者/读者索取更多资源

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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