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Ice-binding proteins from sea ice diatoms (Bacillariophyceae)

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Cited 117 time in scopus
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Ice-binding proteins from sea ice diatoms (Bacillariophyceae)
Other Titles
해빙 규조류의 얼음활성 단백질 연구
A Krell
T Mock
MG. Janech
JA Raymond
Kang, Jae-Shin
Science & Technology - Other Topics
IBP; ice-binding protein
Issue Date
A Krell, et al. 2006. "Ice-binding proteins from sea ice diatoms (Bacillariophyceae)". Journal of Phycology, 42(1): 410-416.
Sea ice diatoms thrive under conditions of low temperature and high salinity, and as a result are responsible for a significant fraction of polar photosynthesis. Their success may be owing in part to secretion of macromolecules that have previously been shown to interfere with the growth of ice and to have the ability to act as cryoprotectants. Here we show that one of these molecules, produced by the sea ice diatom Navicula glaciei Vanheurk, is a similar to 25 kDa ice-binding protein (IBP). A cDNA obtained from another sea ice diatom, Fragilariopsis cylindrus Grunow, was found to encode a protein that closely matched the partially sequenced N. glaciei IBP, and enabled the amplification and sequencing of an N. glaciei IBP cDNA. Similar proteins are not present in the genome of the mesophilic diatom Thalassiosira pseudonana. Both proteins closely resemble antifreeze proteins from psychrophilic snow molds, and as a group represent a new class of IBPs that is distinct from other IBPs found in fish, insects and plants, and bacteria. The diatom IBPs also have striking similarities to three prokaryotic hypothetical proteins. Relatives of both snow molds and two of the prokaryotes have been found in sea ice, raising the possibility of a fungal or bacterial origin of diatom IBPs.
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