In Arabidopsis, there are at least seven class I acylhydrolase members, which have a putative N-terminal chloroplast-targeting signal. Here, we show that all seven class I proteins are localized to the chloroplasts and hydrolyze phosphatidylcholine at the sn-1 position. However, based on their activities toward various lipids, Arabidopsis class I enzymes could be further divided into three sub-groups by substrate specificity, one with phospholipase-specific activity, another with phospholipase and galactolipase activities, and the other with broad lipolytic activity toward phosphatidylcholine, galactolipids, and triacylglycerol. These results suggest that the three sub-groups of class I acylhydrolases have specific roles in chloroplasts.
Bibliographical noteFunding Information:
This work was supported by grants from the Plant Diversity Research Center (21st Century Frontier Research Program funded by the Ministry of Education, Science, and Technology), the Korea Science and Engineering Foundation (Project No. R01-2008-000-20648-0), and the Technology Development Program for Agriculture and Forestry (Project No. 309017-5 funded by the Ministry for Agriculture, Forestry and Fisheries, Republic of Korea). Y.S.S. was recipients of Brain Korea (BK21) research assistant professor scholarships.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology