Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne |
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Authors: | Kumble Krishnanand D Demmer Jerome Fish Steven Hall Claire Corrales Sofia DeAth Angela Elton Clare Prestidge Ross Luxmanan Selvanesan Marshall Craig J Wharton David A |
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Institution: | aGenesis Research and Development Corporation Limited, One Fox Street, Parnell, Auckland 1052, New Zealand;bDepartment of Biochemistry, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand;cDepartment of Zoology, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand |
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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 IAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3. |
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Keywords: | Antifreeze protein Recrystallization inhibition Thermal hysteresis Ice nucleation Ryegrass Lolium perenne Ice-active protein |
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