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Separate origins of ice-binding proteins in antarctic chlamydomonas species.

PLoS ONE. 2013; 
RaymondJames A,Morgan-KissRac
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Codon Optimization … of one of the IBP isoforms (without the signal peptide) was sent to GenScript (Piscataway, NJ) for expression of recombinant protein. The nucleotide sequence was optimized for E. coli codons (Fig. S1), modified to encode an N-terminal His-tag, and expressed in E. coli using the … Get A Quote

摘要

The green alga Chlamydomonas raudensis is an important primary producer in a number of ice-covered lakes and ponds in Antarctica. A C. raudensis isolate (UWO241) from Lake Bonney in the McMurdo Dry Valleys, like many other Antarctic algae, was found to secrete ice-binding proteins (IBPs), which appear to be essential for survival in icy environments. The IBPs of several Antarctic algae (diatoms, a prymesiophyte, and a prasinophyte) are similar to each other (here designated as type I IBPs) and have been proposed to have bacterial origins. Other IBPs (type II IBPs) that bear no resemblance to type I IBPs, have been found in the Antarctic Chlamydomonas sp. CCMP681, a putative snow alga, raising th... More

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