KOPRI Repository

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

Cited 2 time in wos
Cited 1 time in scopus

Full metadata record

DC Field Value Language
dc.contributor.authorHwang, Jisub-
dc.contributor.authorKim, Bomi-
dc.contributor.authorLee, Min Ju-
dc.contributor.authorKim, Eun Jae-
dc.contributor.authorCho, Sung Mi-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorHan, Se Jong-
dc.contributor.authorKim, Kitae-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorDo, Hackwon-
dc.date.accessioned2022-07-29T04:53:24Z-
dc.date.available2022-07-29T04:53:24Z-
dc.date.issued2022-04-15-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/13712-
dc.description.abstractIce-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.en_US
dc.languageEnglishen_US
dc.language.isoenen_US
dc.subjectBiochemistry & Molecular Biologyen_US
dc.subjectChemistryen_US
dc.subjectPolymer Scienceen_US
dc.subject.classification해당사항없음en_US
dc.titleImportance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survivalen_US
dc.title.alternative고활성 및 미생물 생존을 위한 결빙방지 단백질(FfIBP)의 강성의 중요성en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationHwang, Jisub, et al. 2022. "Importance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survival". <em>INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES</em>, 204: 485-499.-
dc.citation.titleINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULESen_US
dc.citation.volume204en_US
dc.identifier.doi10.1016/j.ijbiomac.2022.02.032-
dc.citation.startPage485en_US
dc.citation.endPage499en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2020:6.667en_US
dc.subject.keywordPolar microorganismsen_US
dc.subject.keywordIce binding proteinsen_US
dc.subject.keywordCold adaptationen_US
dc.identifier.localId2022-0021-
dc.identifier.scopusid2-s2.0-85124478108-
dc.identifier.wosid000784299000002-
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)
Files in This Item

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse