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Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region

Cited 2 time in scopus
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Title
Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region
Other Titles
남극 규조 케토세로스 네오그라실의 결빙방지 단백질의 아이소폼의 발굴, 특성연구 및 단백질 코어구조의 중요성 제안
Authors
Kim, Minjae
Jin, EonSeon
Jung, Woongsic
Gwak, Yunho
Subject
Pharmacology & Pharmacy
Keywords
3D-structure modeling; Antarctic marine diatom; Chaetoceros neogracile; antifreeze activity; isoform antifreeze protein
Issue Date
2017
Citation
Kim, Minjae, et al. 2017. "Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region". MARINE DRUGS, 15(10): 318-318.
Abstract
Antifreeze proteins (AFPs) protecting the cells against freezing are produced in response to extremely low temperatures in diverse psychrophilic organisms, and they are encoded by multiple gene families. The AFP of Antarctic marine diatom Chaetoceros neogracile is reported in our previous research, but like other microalgae, was considered to probably have additional genes coding AFPs. In this paper, we reported the cloning and characterization of additional AFP gene from C. neogracile (Cn-isoAFP). Cn-isoAFP protein is 74.6% identical to the previously reported Cn-AFP. The promoter sequence of Cn-isoAFP contains environmental stress responsive elements for cold, thermal, and high light conditions. Cn-isoAFP transcription levels increased dramatically when cells were exposed to freezing (-20 oC), thermal (10 oC), or high light (600 umol photon m-2 s-1) stresses. The thermal hysteresis (TH) activity of recombinant Cn-isoAFP was 0.8 oC at a protein concentration of 5 mg/mL. Results from homology modeling and TH activity analysis of site-directed mutant proteins elucidated AFP mechanism to be a result of flatness of B-face maintained via hydrophobic interactions.
URI
http://repository.kopri.re.kr/handle/201206/6517
DOI
http://dx.doi.org/10.3390/md15100318
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