Back to Search
Start Over
An intracellular antifreeze protein from an Antarctic microalga that responds to various environmental stresses
- Source :
- The FASEB Journal. 28:4924-4935
- Publication Year :
- 2014
- Publisher :
- Wiley, 2014.
-
Abstract
- The structure and function of the Antarctic marine diatom Chaetoceros neogracile antifreeze protein (Cn-AFP), as well as its expression levels and characteristics of the ice-binding site, were analyzed in the present study. In silico analysis revealed that the Cn-AFP promoter contains both light- and temperature-responsive elements. Northern and Western blot analyses demonstrated that both Cn-AFP transcript and protein expression were strongly and rapidly stimulated by freezing, as well as temperature and high light stress. Immunogold labeling revealed that Cn-AFP is preferentially localized to the intracellular space near the chloroplast membrane. Recombinant Cn-AFP had clear antifreeze activity. Protein-folding simulation was used to predict the putative ice-binding sites in Cn-AFP, and site-directed mutagenesis of the Cn-AFP b-face confirmed their identification.
- Subjects :
- Models, Molecular
Protein Folding
In silico
Biology
Biochemistry
Chloroplast membrane
Protein Structure, Secondary
law.invention
Western blot
Stress, Physiological
Antifreeze protein
law
Antifreeze Proteins
Botany
Microalgae
Genetics
medicine
neoplasms
Molecular Biology
Binding Sites
medicine.diagnostic_test
Ice
digestive, oral, and skin physiology
Mutagenesis
Immunogold labelling
Recombinant Proteins
digestive system diseases
embryonic structures
Mutagenesis, Site-Directed
Recombinant DNA
Crystallization
Intracellular
Biotechnology
Subjects
Details
- ISSN :
- 15306860 and 08926638
- Volume :
- 28
- Database :
- OpenAIRE
- Journal :
- The FASEB Journal
- Accession number :
- edsair.doi.dedup.....5627683ff0082b1a3aaf3724bbee7303