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Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive

A supersoluble 40-residue type I antifreeze protein (AFP) was discovered in a righteye flounder, the barfin plaice (bp). Unlike all other AFPs characterized to date, bpAFP transitions from moderately-active to hyperactive with increasing concentration. At sub-mM concentrations, bpAFP bound to pyrami...

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Autores principales: Mahatabuddin, Sheikh, Hanada, Yuichi, Nishimiya, Yoshiyuki, Miura, Ai, Kondo, Hidemasa, Davies, Peter L., Tsuda, Sakae
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5304152/
https://www.ncbi.nlm.nih.gov/pubmed/28211917
http://dx.doi.org/10.1038/srep42501
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author Mahatabuddin, Sheikh
Hanada, Yuichi
Nishimiya, Yoshiyuki
Miura, Ai
Kondo, Hidemasa
Davies, Peter L.
Tsuda, Sakae
author_facet Mahatabuddin, Sheikh
Hanada, Yuichi
Nishimiya, Yoshiyuki
Miura, Ai
Kondo, Hidemasa
Davies, Peter L.
Tsuda, Sakae
author_sort Mahatabuddin, Sheikh
collection PubMed
description A supersoluble 40-residue type I antifreeze protein (AFP) was discovered in a righteye flounder, the barfin plaice (bp). Unlike all other AFPs characterized to date, bpAFP transitions from moderately-active to hyperactive with increasing concentration. At sub-mM concentrations, bpAFP bound to pyramidal planes of ice to shape it into a bi-pyramidal hexagonal trapezohedron, similarly to the other moderately-active AFPs. At mM concentrations, bpAFP uniquely underwent further binding to the whole ice crystal surface including the basal planes. The latter caused a bursting ice crystal growth normal to c-axis, 3 °C of high thermal hysteresis, and alteration of an ice crystal into a smaller lemon-shaped morphology, all of which are well-known properties of hyperactive AFPs. Analytical ultracentrifugation showed this activity transition is associated with oligomerization to form tetramer, which might be the forerunner of a naturally occurring four-helix-bundle AFP in other flounders.
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spelling pubmed-53041522017-03-14 Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive Mahatabuddin, Sheikh Hanada, Yuichi Nishimiya, Yoshiyuki Miura, Ai Kondo, Hidemasa Davies, Peter L. Tsuda, Sakae Sci Rep Article A supersoluble 40-residue type I antifreeze protein (AFP) was discovered in a righteye flounder, the barfin plaice (bp). Unlike all other AFPs characterized to date, bpAFP transitions from moderately-active to hyperactive with increasing concentration. At sub-mM concentrations, bpAFP bound to pyramidal planes of ice to shape it into a bi-pyramidal hexagonal trapezohedron, similarly to the other moderately-active AFPs. At mM concentrations, bpAFP uniquely underwent further binding to the whole ice crystal surface including the basal planes. The latter caused a bursting ice crystal growth normal to c-axis, 3 °C of high thermal hysteresis, and alteration of an ice crystal into a smaller lemon-shaped morphology, all of which are well-known properties of hyperactive AFPs. Analytical ultracentrifugation showed this activity transition is associated with oligomerization to form tetramer, which might be the forerunner of a naturally occurring four-helix-bundle AFP in other flounders. Nature Publishing Group 2017-02-13 /pmc/articles/PMC5304152/ /pubmed/28211917 http://dx.doi.org/10.1038/srep42501 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Mahatabuddin, Sheikh
Hanada, Yuichi
Nishimiya, Yoshiyuki
Miura, Ai
Kondo, Hidemasa
Davies, Peter L.
Tsuda, Sakae
Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title_full Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title_fullStr Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title_full_unstemmed Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title_short Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
title_sort concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5304152/
https://www.ncbi.nlm.nih.gov/pubmed/28211917
http://dx.doi.org/10.1038/srep42501
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