globalchange  > 过去全球变化的重建
DOI: 10.1371/journal.pone.0154056
论文题名:
New Cysteine-Rich Ice-Binding Protein Secreted from Antarctic Microalga, Chloromonas sp.
作者: Woongsic Jung; Robert L. Campbell; Yunho Gwak; Jong Im Kim; Peter L. Davies; EonSeon Jin
刊名: PLOS ONE
ISSN: 1932-6203
出版年: 2016
发表日期: 2016-4-20
卷: 11, 期:4
语种: 英语
英文关键词: Antifreeze proteins ; Sequence alignment ; Sea ice ; Sequence motif analysis ; Antarctica ; DNA sequence analysis ; Sequence databases ; Protein structure
英文摘要: Many microorganisms in Antarctica survive in the cold environment there by producing ice-binding proteins (IBPs) to control the growth of ice around them. An IBP from the Antarctic freshwater microalga, Chloromonas sp., was identified and characterized. The length of the Chloromonas sp. IBP (ChloroIBP) gene was 3.2 kb with 12 exons, and the molecular weight of the protein deduced from the ChloroIBP cDNA was 34.0 kDa. Expression of the ChloroIBP gene was up- and down-regulated by freezing and warming conditions, respectively. Western blot analysis revealed that native ChloroIBP was secreted into the culture medium. This protein has fifteen cysteines and is extensively disulfide bonded as shown by in-gel mobility shifts between oxidizing and reducing conditions. The open-reading frame of ChloroIBP was cloned and over-expressed in Escherichia coli to investigate the IBP’s biochemical characteristics. Recombinant ChloroIBP produced as a fusion protein with thioredoxin was purified by affinity chromatography and formed single ice crystals of a dendritic shape with a thermal hysteresis activity of 0.4±0.02°C at a concentration of 5 mg/ml. In silico structural modeling indicated that the three-dimensional structure of ChloroIBP was that of a right-handed β-helix. Site-directed mutagenesis of ChloroIBP showed that a conserved region of six parallel T-X-T motifs on the β-2 face was the ice-binding region, as predicted from the model. In addition to disulfide bonding, hydrophobic interactions between inward-pointing residues on the β-1 and β-2 faces, in the region of ice-binding motifs, were crucial to maintaining the structural conformation of ice-binding site and the ice-binding activity of ChloroIBP.
URL: http://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0154056&type=printable
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/23687
Appears in Collections:过去全球变化的重建
影响、适应和脆弱性
科学计划与规划
气候变化与战略
全球变化的国际研究计划
气候减缓与适应
气候变化事实与影响

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作者单位: Department of Life Science, Hanyang University, Seoul, South Korea;Department of Biomedical and Molecular Sciences, Queen’s University, Kingston, Canada K7L-3N6;Department of Life Science, Hanyang University, Seoul, South Korea;Department of Biology, Chungnam National University, Daejeon, South Korea;Department of Biomedical and Molecular Sciences, Queen’s University, Kingston, Canada K7L-3N6;Department of Life Science, Hanyang University, Seoul, South Korea

Recommended Citation:
Woongsic Jung,Robert L. Campbell,Yunho Gwak,et al. New Cysteine-Rich Ice-Binding Protein Secreted from Antarctic Microalga, Chloromonas sp.[J]. PLOS ONE,2016-01-01,11(4)
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