Abstract

Several cold-hardy grasses have been shown to have ice-binding proteins (IBPs) that protect against freeze-thaw injury. Here, we looked for IBP activity in an Alaskan coastal grass, Leymus mollis (Pooidae), that had not previously been examined. Rhizome tissue had strong ice-structuring and ice recrystallization inhibiting (IRI) activities, indicating the probable presence of IBPs. The gene sequence of an IBP was obtained. The sequence encoded a 118-amino acid IRI domain composed of eight repeats and that was 80% identical to the IRI domain of the IBP of perennial ryegrass Lolium perenne. The predicted 3D structure of the IRI domain had eight beta-roll coils like those in L. perenne IBP.

Highlights

  • Several cold-hardy grasses have been shown to have ice-binding proteins (IBPs) that protect against freeze-thaw injury

  • The IBPs, which have negligible effect on the freezing point, are characterized by a C-terminal domain consisting of several repeating units that is associated with strong ice recrystallization inhibition (IRI) activity (Sandve et al, 2008)

  • Among the Pooidae, L. mollis is a member of the Triticodae, which includes wheat (Triticum) and barley (Hordeum), while Lolium and Deschampsia are members of the Poodae

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Summary

Introduction

Several cold-hardy grasses have been shown to have ice-binding proteins (IBPs) that protect against freeze-thaw injury. Keywords Leymus mollis, ice-binding protein, Arctic, Alaska, Pooidae, dune grass, Chukchi Sea version 2 (revision) These grasses have developed a large family of ice-binding proteins (IBPs) that protect the plants from freezing damage (Sandve et al, 2008).

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