Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 79, Issue 7, Pages 1119-1124Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2015.1010480
Keywords
microalga; caleosin; oil body protein; salt stress; Chlorella vulgaris
Categories
Funding
- Ministry of Education, Science and Culture of Japan
- International Research Center for Natural Environmental Science of Meijo University
- Grants-in-Aid for Scientific Research [15K18743] Funding Source: KAKEN
Ask authors/readers for more resources
Physiological and functional properties of lipid droplet-associated proteins in algae remain scarce. We report here the caleosin gene from Chlorella vulgaris encodes a protein of 279 amino acid residues. Amino acid sequence alignment showed high similarity to the putative caleosins from fungi, but less to plant caleosins. When the C. vulgaris TISTR 8580 cells were treated with salt stress (0.3M NaCl), the level of triacylglycerol increased significantly. The mRNA contents for caleosin in Chlorella cells significantly increased under salt stress condition. Caleosin gene was expressed in E. coli. Crude extract of E. coli cells exhibited the cumene hydroperoxide-dependent oxidation of aniline. Absorption spectroscopy showed a peak around 415nm which was decreased upon addition of cumene hydroperoxide. Native polyacrylamide gel electrophoresis suggests caleosin existed as the oligomer. These data indicate that a fresh water C. vulgaris TISTR 8580 contains a salt-induced heme-protein caleosin.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available