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Importance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survival

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Title
Importance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survival
Other Titles
고활성 및 미생물 생존을 위한 결빙방지 단백질(FfIBP)의 강성의 중요성
Authors
Hwang, Jisub
Kim, Bomi
Lee, Min Ju
Kim, Eun Jae
Cho, Sung Mi
Lee, Sung Gu
Han, Se Jong
Kim, Kitae
Lee, Jun Hyuck
Do, Hackwon
Subject
Biochemistry & Molecular BiologyChemistryPolymer Science
Keywords
Polar microorganismsIce binding proteinsCold adaptation
Issue Date
2022-04-15
Citation
Hwang, Jisub, et al. 2022. "Importance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survival". INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 204: 485-499.
Abstract
Ice-binding proteins (IBPs) are well-characterized proteins responsible for the cold-adaptation mechanisms. Despite extensive structural and biological investigation of IBPs and antifreeze proteins, only a few studies have considered the relationship between protein stabilization and thermal hysteresis (TH) activity as well as the implication of hyperactivity. Here, we investigated the important role of the head capping region in stabilization and the hyper-TH activity of FfIBP using molecular dynamics simulation. Data comparison revealed that residues on the ice-binding site of the hyperactive FfIBP are immobilized, which could be correlated with TH activity. Further comparison analysis indicated the disulfide bond in the head region is mainly involved in protein stabilization and is crucial for hyper-TH activity. This finding could also be generalized to known hyperactive IBPs. Furthermore, in mimicking the physiological conditions, bacteria with membrane-anchored FfIBP formed brine pockets in a TH activity-dependent manner. Cells with a higher number of TH-active IBPs showed an increased number of brine pockets, which may be beneficial for short- and long-term survival in cold environments by reducing the salt concentration. The newly identified conditions for hyper-TH activity and their implications on bacterial survival provide insights into novel mechanistic aspects of cold adaptation in polar microorganisms.
URI
https://repository.kopri.re.kr/handle/201206/13712
DOI
http://dx.doi.org/10.1016/j.ijbiomac.2022.02.032
Type
Article
Station
해당사항없음
Indexed
SCIE
Appears in Collections  
2022-2022, Development of potential antibiotic compounds using polar organism resources (22-22) / Lee, Jun Hyuck (PM22030)
2022-2022, Investigation of ice microstructure properties for developing low-temperature purification and environment/energy materials (22-22) / Kim, Kitae (PE22120)
2022-2022, Post-Polar Genomics Project: Functional genomic study for securing of polar useful genes (22-22) / Kim, Jin-Hyoung (PE22160)
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