Intrinsically disordered stress protein COR15A resides at the membrane surface during dehydration

Simple item page
dc.contributor.authorBremer, Aen_AU
dc.contributor.authorKent, Ben_AU
dc.contributor.authorHauß, Ten_AU
dc.contributor.authorThalhammer, Aen_AU
dc.contributor.authorYepuri, NRen_AU
dc.contributor.authorDarwish, TAen_AU
dc.contributor.authorGarvey, CJen_AU
dc.contributor.authorBryant, Gen_AU
dc.contributor.authorHincha, DKen_AU
dc.date.accessioned2021-01-11T01:56:53Zen_AU
dc.date.available2021-01-11T01:56:53Zen_AU
dc.date.issued2017-08-08en_AU
dc.date.statistics2021-01-08en_AU
dc.description.abstractPlants from temperate climate zones are able to increase their freezing tolerance during exposure to low, above-zero temperatures in a process termed cold acclimation. During this process, several cold-regulated (COR) proteins are accumulated in the cells. One of them is COR15A, a small, intrinsically disordered protein that contributes to leaf freezing tolerance by stabilizing cellular membranes. The isolated protein folds into amphipathic α-helices in response to increased crowding conditions, such as high concentrations of glycerol. Although there is evidence for direct COR15A-membrane interactions, the orientation and depth of protein insertion were unknown. In addition, although folding due to high osmolyte concentrations had been established, the folding response of the protein under conditions of gradual dehydration had not been investigated. Here we show, using Fourier transform infrared spectroscopy, that COR15A starts to fold into α-helices already under mild dehydration conditions (97% relative humidity (RH), corresponding to freezing at −3°C) and that folding gradually increases with decreasing RH. Neutron diffraction experiments at 97 and 75% RH established that the presence of COR15A had no significant influence on the structure of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membranes. However, using deuterated POPC we could clearly establish that COR15A interacts with the membranes and penetrates below the headgroup region into the upper part of the fatty acyl chain region. This localization is in agreement with our hypothesis that COR15A-membrane interaction is at least, in part, driven by a hydrophobic interaction between the lipids and the hydrophobic face of the amphipathic protein α-helix. © 2017 Biophysical Society - Open accessen_AU
dc.identifier.citationBremer, A., Kent, B., Hauß, T., Thalhammer, A., Yepuri, N. R., Darwish, T. A., Garvey, C, J., Bryant, G., & Hincha, D. K. (2017). Intrinsically disordered stress protein COR15A resides at the membrane surface during dehydration. Biophysical Journal, 113(3), 572-579. doi:10.1016/j.bpj.2017.06.027en_AU
dc.identifier.issn0006-3495en_AU
dc.identifier.issue3en_AU
dc.identifier.journaltitleBiophysical Journalen_AU
dc.identifier.pagination572-579en_AU
dc.identifier.urihttps://doi.org/10.1016/j.bpj.2017.06.027en_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/10232en_AU
dc.identifier.volume113en_AU
dc.language.isoenen_AU
dc.publisherBiophysical Societyen_AU
dc.subjectProteinsen_AU
dc.subjectPlantsen_AU
dc.subjectTemperature range 0065-0273 Ken_AU
dc.subjectCell membranesen_AU
dc.subjectGlycerolen_AU
dc.subjectSurface propertiesen_AU
dc.subjectLecithinsen_AU
dc.titleIntrinsically disordered stress protein COR15A resides at the membrane surface during dehydrationen_AU
dc.typeJournal Articleen_AU
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
1-s2.0-S000634951730677X-main.pdf
Size:
594.84 KB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.63 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Journal Articles