Type II fish antifreeze protein accumulation in transgenic tobacco does not confer frost resistance.
作者： Kimberly D. Kenward , James Brandle , Joan McPherson , Peter L. Davies
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摘要: Type II fish antifreeze protein (AFP) is active in both freezing point depression and the inhibition of ice recrystallization. This extensively disulfide-bonded 14 kDa was targeted for accumulation its pro- mature forms cytosol apoplast transgenic tobacco plants. AFP gene constructs under control a duplicate cauliflower mosaic virus 35S promoter, with without native plant transit peptide sequence, were introduced into by Agrobacterium tumefaciens-mediated transformation. did not accumulate plants, but present as 2% total apoplast. Plant-produced same size isolated from fish, comparable to wild-type thermal hysteresis activity effect on crystal morphology. Field trials conducted late summer R1 generation plants showed similar field conditions at levels suitable large-scale production: no difference frost resistance observed between during onset early fall frosts.
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sci-hub.se 参考文章(53)
P. A. Negulescu, B. Rubinsky, G. L. Fletcher, T. E. Machen, Fish antifreeze proteins block Ca entry into rabbit parietal cells. American Journal of Physiology-cell Physiology. ,vol. 263, ,(1992) , 10.1152/AJPCELL.1992.263.6.C1310
Bernard P. Duncker, Peter L. Davies, Virginia K. Walker, Increased gene dosage augments antifreeze protein levels in transgenic Drosophila melanogaster. Transgenic Research. ,vol. 8, pp. 45- 50 ,(1999) , 10.1023/A:1008873906177
A. J. J. van Ooijen, A. Hoekema, A. Hiatt, P. C. Sijmons, J. Pen, Protein production in transgenic crops: analysis of plant molecular farming. Marcel Dekker. pp. 239- 251 ,(1993)
Peter Gegengeimer, Preparation of extracts from plants. Methods in Enzymology. ,vol. 182, pp. 174- 193 ,(1990) , 10.1016/0076-6879(90)82016-U
V.S. Ananthanarayanan, Choy L. Hew, Structural studies on the freezing-point-depressing protein of the winter flounder Pseudopleuronectes americanus Biochemical and Biophysical Research Communications. ,vol. 74, pp. 685- 689 ,(1977) , 10.1016/0006-291X(77)90357-6
P H Hayes, G K Scott, N F Ng, C L Hew, P L Davies, Cystine-rich type II antifreeze protein precursor is initiated from the third AUG codon of its mRNA. Journal of Biological Chemistry. ,vol. 264, pp. 18761- 18767 ,(1989) , 10.1016/S0021-9258(18)51532-5
C L Hew, N C Wang, S Joshi, G L Fletcher, G K Scott, P H Hayes, B Buettner, P L Davies, Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus. Journal of Biological Chemistry. ,vol. 263, pp. 12049- 12055 ,(1988) , 10.1016/S0021-9258(18)37891-8
D Wen, R.A. Laursen, Structure-function relationships in an antifreeze polypeptide. The role of neutral, polar amino acids. Journal of Biological Chemistry. ,vol. 267, pp. 14102- 14108 ,(1992) , 10.1016/S0021-9258(19)49684-1
James G. Wallis, Hongyu Wang, Daniel J. Guerra*, Expression of a synthetic antifreeze protein in potato reduces electrolyte release at freezing temperatures Plant Molecular Biology. ,vol. 35, pp. 323- 330 ,(1997) , 10.1023/A:1005886210159
Wai-Ching Hon, Marilyn Griffith, Pele Chong, Daniel SC Yang, Extraction and Isolation of Antifreeze Proteins from Winter Rye (Secale cereale L.) Leaves. Plant Physiology. ,vol. 104, pp. 971- 980 ,(1994) , 10.1104/PP.104.3.971