A carrot leucine-rich-repeat protein that inhibits ice recrystallization

D Worrall; L Elias; D Ashford; M Smallwood; C Sidebottom; P Lillford; J Telford; C Holt; D Bowles

doi:10.1126/science.282.5386.115

A carrot leucine-rich-repeat protein that inhibits ice recrystallization

D Worrall, L Elias, D Ashford, M Smallwood, C Sidebottom, P Lillford, J Telford, C Holt, D Bowles

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Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	115-117
Number of pages	3
Journal	Science
Volume	282
Issue number	5386
DOIs	https://doi.org/10.1126/science.282.5386.115
Publication status	Published - 2 Oct 1998

Keywords

THERMAL HYSTERESIS PROTEIN
ANTIFREEZE PROTEINS
CRYSTAL-STRUCTURE
PLANTS
ELECTROPHORESIS
PATHOGENESIS
EXPRESSION
BINDING
TOMATO

Access to Document

10.1126/science.282.5386.115

http://www.ncbi.nlm.nih.gov/pubmed/9756474

Cite this

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title = "A carrot leucine-rich-repeat protein that inhibits ice recrystallization",

abstract = "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.",

keywords = "THERMAL HYSTERESIS PROTEIN, ANTIFREEZE PROTEINS, CRYSTAL-STRUCTURE, PLANTS, ELECTROPHORESIS, PATHOGENESIS, EXPRESSION, BINDING, TOMATO",

author = "D Worrall and L Elias and D Ashford and M Smallwood and C Sidebottom and P Lillford and J Telford and C Holt and D Bowles",

year = "1998",

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doi = "10.1126/science.282.5386.115",

language = "English",

volume = "282",

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journal = "Science",

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publisher = "American Association for the Advancement of Science",

number = "5386",

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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 - Article

SN - 0036-8075

VL - 282

SP - 115

EP - 117

JO - Science

JF - Science

IS - 5386

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