Academic literature on the topic 'Strawberry; Antifreeze protein gene'

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Journal articles on the topic "Strawberry; Antifreeze protein gene"

1

Firsov, A. P., and S. V. Dolgov. "AGROBACTERIAL TRANSFORMATION AND TRANSFER OF THE ANTIFREEZE PROTEIN GENE OF WINTER FLOUNDER TO THE STRAWBERRY." Acta Horticulturae, no. 484 (December 1998): 581–86. http://dx.doi.org/10.17660/actahortic.1998.484.99.

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2

Scott, Gary K., Garth L. Fletcher, and Peter L. Davies. "Fish Antifreeze Proteins: Recent Gene Evolution." Canadian Journal of Fisheries and Aquatic Sciences 43, no. 5 (1986): 1028–34. http://dx.doi.org/10.1139/f86-128.

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A variety of antifreeze proteins is produced by marine teleosts inhabiting polar regions to ensure protection from internal ice formation at subzero temperatures. Combining evidence from paleoclimatology, teleostian evolution, and studies of antifreeze gene organization, the case is made for Cenozoic cooling as the force driving antifreeze evolution in marine teleosts. The distribution of antifreeze types amongst teleost suborders, families, genera, and species correlates with Cenozoic glaciation in the Southern Hemisphere preceding that in the Northern Hemisphere by approximately 25 million yr. The genomic organization of antifreeze genes suggests recent and extensive amplification, an event compatible with their proposed stress-induced origin. Also, a realignment of the nototheniids with the Gadiformes based on antifreeze protein data is suggested.
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3

Gauthier, Sherry, Yaling Wu, and Peter L. Davies. "Nucleotide sequence of a variant antifreeze protein gene." Nucleic Acids Research 18, no. 17 (1990): 5303. http://dx.doi.org/10.1093/nar/18.17.5303.

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4

Qin, Wensheng, and Virginia K. Walker. "Tenebrio molitor antifreeze protein gene identification and regulation." Gene 367 (February 2006): 142–49. http://dx.doi.org/10.1016/j.gene.2005.10.003.

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5

Fletcher, Garth L., David R. Idler, Allan Vaisius, and Choy L. Hew. "Hormonal regulation of antifreeze protein gene expression in winter flounder." Fish Physiology and Biochemistry 7, no. 1-6 (1989): 387–93. http://dx.doi.org/10.1007/bf00004733.

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6

Davies, Peter L., Choy L. Hew, and Garth L. Fletcher. "Fish antifreeze proteins: physiology and evolutionary biology." Canadian Journal of Zoology 66, no. 12 (1988): 2611–17. http://dx.doi.org/10.1139/z88-385.

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Many marine teleosts have adapted to ice-laden seawater by evolving antifreeze proteins and glycoproteins. These proteins are synthesized in the liver for export to the blood where they circulate at levels of up to 20 mg/mL. There are at least four distinct antifreeze protein classes differing in carbohydrate content, amino acid composition, protein sequence, and secondary structure. In addition to antifreeze structural diversity, fish species differ considerably with respect to mechanisms controlling seasonal regulation of plasma antifreeze concentrations. Some species synthesize antifreeze proteins immediately before the onset of freezing conditions, some synthesize them in response to such conditions, whereas others possess high concentrations all year. Endogenous rhythms, water temperature, photoperiod, and pituitary hormones have all been implicated as regulators of plasma antifreeze protein levels. The structural diversity of antifreeze proteins and their occurrence in a wide range of fish species suggest that they evolved separately and recently during Cenozoic glaciation. Invariably, the genes coding for these antifreeze proteins are amplified, sometimes as long tandem arrays, suggesting intense selective pressure to produce large amounts of protein. The distribution of antifreeze gene types among fish species suggests that they could serve as important tools for studying phylogenetic relationships.
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7

Hobbs, Rod S., Jennifer R. Hall, Laurie A. Graham, Peter L. Davies, and Garth L. Fletcher. "Antifreeze protein dispersion in eelpouts and related fishes reveals migration and climate alteration within the last 20 Ma." PLOS ONE 15, no. 12 (2020): e0243273. http://dx.doi.org/10.1371/journal.pone.0243273.

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Antifreeze proteins inhibit ice growth and are crucial for the survival of supercooled fish living in icy seawater. Of the four antifreeze protein types found in fishes, the globular type III from eelpouts is the one restricted to a single infraorder (Zoarcales), which is the only clade know to have antifreeze protein-producing species at both poles. Our analysis of over 60 unique antifreeze protein gene sequences from several Zoarcales species indicates this gene family arose around 18 Ma ago, in the Northern Hemisphere, supporting recent data suggesting that the Arctic Seas were ice-laden earlier than originally thought. The Antarctic was subject to widespread glaciation over 30 Ma and the Notothenioid fishes that produce an unrelated antifreeze glycoprotein extensively exploited the adjoining seas. We show that species from one Zoarcales family only encroached on this niche in the last few Ma, entering an environment already dominated by ice-resistant fishes, long after the onset of glaciation. As eelpouts are one of the dominant benthic fish groups of the deep ocean, they likely migrated from the north to Antarctica via the cold depths, losing all but the fully active isoform gene along the way. In contrast, northern species have retained both the fully active (QAE) and partially active (SP) isoforms for at least 15 Ma, which suggests that the combination of isoforms is functionally advantageous.
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8

Hew, Choy, Megan Miao, and Garth Fletcher. "Transcriptional regulation of the antifreeze protein gene in the winter flounder." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 124 (August 1999): S4. http://dx.doi.org/10.1016/s1095-6433(99)90012-0.

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9

WANG, Yan. "Cold Tolerance of Transgenic Tobacco Carrying Gene Encoding Insect Antifreeze Protein." ACTA AGRONOMICA SINICA 34, no. 3 (2008): 397–402. http://dx.doi.org/10.3724/sp.j.1006.2008.00397.

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10

Graham, Laurie A., Stephen C. Lougheed, K. Vanya Ewart, and Peter L. Davies. "Lateral Transfer of a Lectin-Like Antifreeze Protein Gene in Fishes." PLoS ONE 3, no. 7 (2008): e2616. http://dx.doi.org/10.1371/journal.pone.0002616.

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