Final published version
Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne
AU - Kumble, Krishnanand D.
AU - Demmer, Jerome
AU - Fish, Steven Anthony
AU - Hall, Claire
AU - Corrales, Sofia
AU - DeAth, Angela
AU - Elton, Clare
AU - Prestidge, Ross
AU - Luxmanan, Selvanesan
AU - Marshall, Craig J.
AU - Wharton, David A.
PY - 2008/12
Y1 - 2008/12
N2 - 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.
AB - 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.
KW - Antifreeze protein
KW - Recrystallization inhibition
KW - Thermal hysteresis
KW - Ice nucleation
KW - Ryegrass
KW - Lolium perenne
KW - Ice-active protein
U2 - 10.1016/j.cryobiol.2008.09.005
DO - 10.1016/j.cryobiol.2008.09.005
M3 - Journal article
VL - 57
SP - 263
EP - 268
JO - Cryobiology
JF - Cryobiology
IS - 3
ER -