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Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne

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  • Krishnanand D. Kumble
  • Jerome Demmer
  • Steven Anthony Fish
  • Claire Hall
  • Sofia Corrales
  • Angela DeAth
  • Clare Elton
  • Ross Prestidge
  • Selvanesan Luxmanan
  • Craig J. Marshall
  • David A. Wharton
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<mark>Journal publication date</mark>12/2008
<mark>Journal</mark>Cryobiology
Issue number3
Volume57
Number of pages6
Pages (from-to)263-268
Publication StatusPublished
Early online date19/09/08
<mark>Original language</mark>English

Abstract

Five genes coding for ice-active proteins were identified from an expressed sequence tag database of Lolium perenne cDNA libraries. Each of the five genes were characterized by the presence of an N-terminal signal peptide, a region enriched in hydrophilic amino acids and a leucine-rich region in four of the five genes that is homologous with the receptor domain of receptor-like protein kinases of plants. The C-terminal region of all five genes contains sequence homologous with Lolium and Triticum ice-active proteins. Of the four ice-active proteins (IAP1, IAP2, IAP3 and IAP5) cloned, three could be expressed in Escherichia coli and recovered in a functional form in order to study their ice activity. All three ice-active proteins had recrystallization inhibition activity but showed no detectable antifreeze or ice nucleation activity at the concentration tested. IAP2 and LAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3.