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

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Title: Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive
Authors: Mahatabuddin, Sheikh Browse this author
Hanada, Yuichi Browse this author
Nishimiya, Yoshiyuki Browse this author
Miura, Ai Browse this author
Kondo, Hidemasa Browse this author
Davies, Peter L. Browse this author
Tsuda, Sakae Browse this author →KAKEN DB
Issue Date: 13-Feb-2017
Publisher: Nature Publishing Group
Journal Title: Scientific reports
Volume: 7
Start Page: 42501
Publisher DOI: 10.1038/srep42501
Abstract: 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 sub-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 degrees 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.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 津田 栄

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