Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
}
TY - JOUR
T1 - A carrot leucine-rich-repeat protein that inhibits ice recrystallization
AU - Worrall, D
AU - Elias, L
AU - Ashford, D
AU - Smallwood, M
AU - Sidebottom, C
AU - Lillford, P
AU - Telford, J
AU - Holt, C
AU - Bowles, D
PY - 1998/10/2
Y1 - 1998/10/2
N2 - Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.
AB - Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.
KW - THERMAL HYSTERESIS PROTEIN
KW - ANTIFREEZE PROTEINS
KW - CRYSTAL-STRUCTURE
KW - PLANTS
KW - ELECTROPHORESIS
KW - PATHOGENESIS
KW - EXPRESSION
KW - BINDING
KW - TOMATO
U2 - 10.1126/science.282.5386.115
DO - 10.1126/science.282.5386.115
M3 - Journal article
VL - 282
SP - 115
EP - 117
JO - Science
JF - Science
SN - 0036-8075
IS - 5386
ER -