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

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Published: 4 June 2021

Last updated: 4 February 2022

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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 y

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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 p

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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 ea

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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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11

Desjardins, Mariève, Laurie A. Graham, Peter L. Davies, and Garth L. Fletcher. "Antifreeze protein gene amplification facilitated niche exploitation and speciation in wolffish." FEBS Journal 279, no. 12 (2012): 2215–30. http://dx.doi.org/10.1111/j.1742-4658.2012.08605.x.

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12

Fletcher, Garth L., Margaret A. Shears, Madonna J. King, Peter L. Davies, and Choy L. Hew. "Evidence for Antifreeze Protein Gene Transfer in Atlantic Salmon (Salmo salar)." Canadian Journal of Fisheries and Aquatic Sciences 45, no. 2 (1988): 352–57. http://dx.doi.org/10.1139/f88-042.

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Atlantic salmon (Salmo salar) freeze to death if they come into contact with ice at water temperatures below −0.7 °C. Consequently, sea-pen culture of this species in cold water is severely limited. Winter flounder (Pseudopleuronectes americanus) survive in ice-laden seawater by producing a set of antifreeze polypeptides (AFP). We are attempting to make the Atlantic salmon more freeze resistant by transferring antifreeze protein genes from the winter flounder to the genome of the salmon. Salmon eggs were microinjected with linearized DNA after fertilization. Individual fingerlings (1–2 g) were

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13

Qin, Wensheng, Michael G. Tyshenko, Daniel Doucet, and Virginia K. Walker. "Characterization of antifreeze protein gene expression in summer spruce budworm larvae." Insect Biochemistry and Molecular Biology 36, no. 3 (2006): 210–18. http://dx.doi.org/10.1016/j.ibmb.2006.01.017.

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14

Yamazaki, Aya, Yoshiyuki Nishimiya, Sakae Tsuda, Koji Togashi, and Hiroyuki Munehara. "Freeze Tolerance in Sculpins (Pisces; Cottoidea) Inhabiting North Pacific and Arctic Oceans: Antifreeze Activity and Gene Sequences of the Antifreeze Protein." Biomolecules 9, no. 4 (2019): 139. http://dx.doi.org/10.3390/biom9040139.

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Many marine species inhabiting icy seawater produce antifreeze proteins (AFPs) to prevent their body fluids from freezing. The sculpin species of the superfamily Cottoidea are widely found from the Arctic to southern hemisphere, some of which are known to express AFP. Here we clarified DNA sequence encoding type I AFP for 3 species of 2 families (Cottidae and Agonidae) belonging to Cottoidea. We also examined antifreeze activity for 3 families and 32 species of Cottoidea (Cottidae, Agonidae, and Rhamphocottidae). These fishes were collected in 2013–2015 from the Arctic Ocean, Alaska, Japan. We

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15

SMALLWOOD, Maggie, Dawn WORRALL, Louise BYASS, et al. "Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)." Biochemical Journal 340, no. 2 (1999): 385–91. http://dx.doi.org/10.1042/bj3400385.

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A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants. This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N-glycosylated. The corresponding gene is unique in the carrot genome and induced by cold. The antifreeze protein appears to be localized within the apoplast.

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16

Murray, Harry M., Choy L. Hew, Ken R. Kao, and Garth L. Fletcher. "Localization of cells from the winter flounder gill expressing a skin type antifreeze protein gene." Canadian Journal of Zoology 80, no. 1 (2002): 110–19. http://dx.doi.org/10.1139/z01-209.

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In situ hybridization on whole mounts and paraffin-sectioned winter flounder (Pleuronectes americanus) gill, using riboprobes specific to a skin type antifreeze protein (AFP) gene, showed a mRNA distribution associated with cells throughout the filament and the lamellae. Immunohistochemistry using antibodies for a skin-type AFP identified cells corresponding to those detected using in situ hybridization. Parallel experiments with antibodies for chloride-cell markers showed that these cells were not involved in antifreeze-protein expression. Similarly, goblet cells did not show cross-reactivity

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17

Hayes, Pliny H., Peter L. Davies, and Garth L. Fletcher. "Population differences in antifreeze protein gene copy number and arrangement in winter flounder." Genome 34, no. 1 (1991): 174–77. http://dx.doi.org/10.1139/g91-027.

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Many marine fish in polar waters produce antifreeze proteins (AFPs) to depress their serum freezing point to below that of seawater. Winter flounder from the east coast of North America contain multiple AFP gene copies organized both as tandem repeats and as linked but irregularly spaced genes, with the tandemly repeated genes encoding the bulk of the circulating AFPs. We report here on AFP gene organization in winter flounder from nine locations ranging from Long Island, NY to Conception Bay, Nfld. There are clear differences in AFP gene copy number and arrangement between some of the populat

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18

Young, Heather M., and Garth L. Fletcher. "Antifreeze protein gene expression in winter flounder pre-hatch embryos: Implications for cryopreservation." Cryobiology 57, no. 2 (2008): 84–90. http://dx.doi.org/10.1016/j.cryobiol.2008.05.005.

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19

Zhang, Junfang, Cheng Deng, Jianshe Wang, and Liangbiao Chen. "Identification of a two-domain antifreeze protein gene in Antarctic eelpout Lycodichthys dearborni." Polar Biology 32, no. 1 (2008): 35–40. http://dx.doi.org/10.1007/s00300-008-0499-8.

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20

Wang, Junli, Huibo Ge, Shiqi Peng, Hongmei Zhang, Piling Chen, and Jiuru Xu. "Transformation of strawberry (Fragaria ananassaDuch.) with late embryogenesis abundant protein gene." Journal of Horticultural Science and Biotechnology 79, no. 5 (2004): 735–38. http://dx.doi.org/10.1080/14620316.2004.11511835.

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21

Rancourt, D. E., V. K. Walker, and P. L. Davies. "Flounder antifreeze protein synthesis under heat shock control in transgenic Drosophila melanogaster." Molecular and Cellular Biology 7, no. 6 (1987): 2188–95. http://dx.doi.org/10.1128/mcb.7.6.2188.

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The gene coding for the most abundant antifreeze protein (AFP) in the winter flounder was placed downstream of the Drosophila melanogaster hsp70 promoter and introduced into the D. melanogaster germ line by P-element-mediated transformation. In each of six transgenic strains tested, heat shock treatment induced the expression of two major AFP gene transcripts and one minor one. All three transcripts were spliced despite the lack of an obvious D. melanogaster internal intron-splicing sequence. The variation in transcript length was caused by selection of different polyadenylation sites. Western

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22

Rancourt, D. E., V. K. Walker, and P. L. Davies. "Flounder antifreeze protein synthesis under heat shock control in transgenic Drosophila melanogaster." Molecular and Cellular Biology 7, no. 6 (1987): 2188–95. http://dx.doi.org/10.1128/mcb.7.6.2188-2195.1987.

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The gene coding for the most abundant antifreeze protein (AFP) in the winter flounder was placed downstream of the Drosophila melanogaster hsp70 promoter and introduced into the D. melanogaster germ line by P-element-mediated transformation. In each of six transgenic strains tested, heat shock treatment induced the expression of two major AFP gene transcripts and one minor one. All three transcripts were spliced despite the lack of an obvious D. melanogaster internal intron-splicing sequence. The variation in transcript length was caused by selection of different polyadenylation sites. Western

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23

Muryoi, Naomi, Mika Sato, Shoji Kaneko, et al. "Cloning and Expression of afpA, a Gene Encoding an Antifreeze Protein from the Arctic Plant Growth-Promoting Rhizobacterium Pseudomonas putida GR12-2." Journal of Bacteriology 186, no. 17 (2004): 5661–71. http://dx.doi.org/10.1128/jb.186.17.5661-5671.2004.

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ABSTRACT The Arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2 secretes an antifreeze protein (AFP) that promotes survival at subzero temperatures. The AFP is unusual in that it also exhibits a low level of ice nucleation activity. A DNA fragment with an open reading frame encoding 473 amino acids was cloned by PCR and inverse PCR using primers designed from partial amino acid sequences of the isolated AFP. The predicted gene product, AfpA, had a molecular mass of 47.3 kDa, a pI of 3.51, and no previously known function. Although AfpA is a secreted protein, it lacked an N-

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24

Hobbs, Rod S., and Garth L. Fletcher. "Tissue specific expression of antifreeze protein and growth hormone transgenes driven by the ocean pout (Macrozoarces americanus) antifreeze protein OP5a gene promoter in Atlantic salmon (Salmo salar)." Transgenic Research 17, no. 1 (2007): 33–45. http://dx.doi.org/10.1007/s11248-007-9128-5.

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25

Scott, G. K., P. H. Hayes, G. L. Fletcher, and P. L. Davies. "Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation." Molecular and Cellular Biology 8, no. 9 (1988): 3670–75. http://dx.doi.org/10.1128/mcb.8.9.3670.

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The antifreeze protein genes of the wolffish (Anarhichas lupus) constitute a large multigene family of 80 to 85 copies, which can be classified into two sets. One-third of the genes were linked but irregularly spaced. The other two-thirds were organized as 8-kilobase-pair (kbp) tandem direct repeats that each contained two genes in inverted orientation; DNA sequence analysis suggests that both genes are functional. Except for a single region specific to each gene, the genes and their immediate flanking sequences were 99.2% identical. This degree of identity ended soon after a putative transcri

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26

Scott, G. K., P. H. Hayes, G. L. Fletcher, and P. L. Davies. "Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation." Molecular and Cellular Biology 8, no. 9 (1988): 3670–75. http://dx.doi.org/10.1128/mcb.8.9.3670-3675.1988.

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The antifreeze protein genes of the wolffish (Anarhichas lupus) constitute a large multigene family of 80 to 85 copies, which can be classified into two sets. One-third of the genes were linked but irregularly spaced. The other two-thirds were organized as 8-kilobase-pair (kbp) tandem direct repeats that each contained two genes in inverted orientation; DNA sequence analysis suggests that both genes are functional. Except for a single region specific to each gene, the genes and their immediate flanking sequences were 99.2% identical. This degree of identity ended soon after a putative transcri

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27

Fei Yunbiao, Yu Jiankang, Chen Liangbiao, et al. "Isolation and identification of homologous sequences of antifreeze protein (AFP) gene from a freshwater teleost." Aquaculture 111, no. 1-4 (1993): 306. http://dx.doi.org/10.1016/0044-8486(93)90072-7.

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28

Xiong, Jinsong, Yibo Bai, Chuangju Ma, Hongyu Zhu, Dan Zheng, and Zongming Cheng. "Molecular Cloning and Characterization of SQUAMOSA-Promoter Binding Protein-Like Gene FvSPL10 from Woodland Strawberry (Fragaria vesca)." Plants 8, no. 9 (2019): 342. http://dx.doi.org/10.3390/plants8090342.

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SQUAMOSA-promoter binding protein-like (SPL) proteins are plant-specific transcript factors that play essential roles in plant growth and development. Although many SPL genes have been well characterized in model plants like Arabidopsis, rice and tomato, the functions of SPLs in strawberry are still largely elusive. In the present study, we cloned and characterized FvSPL10, the ortholog of AtSPL9, from woodland strawberry. Subcellular localization shows FvSPL10 localizes in the cell nucleus. The luciferase system assay indicates FvSPL10 is a transcriptional activator, and both in vitro and in

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29

Zhang, Shihong, Yi Wei, and Hongyu Pan. "Transgenic Rice Plants Expressing a Novel Antifreeze Glycopeptide Possess Resistance to Cold and Disease." Zeitschrift für Naturforschung C 62, no. 7-8 (2007): 583–91. http://dx.doi.org/10.1515/znc-2007-7-821.

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Freezing injury and disease are both restrictive factors in crop production. In order to improve the tolerance ability to these stresses, a better way is to carry out genetic engineering by transferring dualfunctional genes. A predicted rice antifreeze glycopeptide gene was purposefully selected from rice blast-induced cDNA library. Northern blot demonstrated that the gene is expressed not only in blast-infected rice leaves, but also in low temperature-treated rice. In addition, the expressed protein in Escherichia coli exhibits strong antifreeze activities. The gene was overexpressed in rice

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30

Wang, Shu-Fang, Li-Na Hua, Xiaofeng Liu, and Yuanyue Shen. "Cloning, expression, and enzymatic activity analysis of strawberry S-adenosyl-L-metnionine synthetase gene FaSAMS1." JOURNAL OF ADVANCES IN AGRICULTURE 6, no. 1 (2016): 841–45. http://dx.doi.org/10.24297/jaa.v6i1.5390.

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The S-adenosyl methionine synthetase gene FaSAMS1 is involved in the regulation of strawberry fruit ripening, however, the biochemical properties of FaSAMS1 protein remain unclear. Here, a coding cDNA sequence of FaSAMS1 was cloned by RT-PCR and inserted into a recombinant yeast expression vector pPICZA, then transformed into the yeast expression strain X-33. The fusion protein FaSAMS1 was induced, expressed, and purified. The enzymatic activity analysis of FaSAMS1 showed that the reaction system contains 0.09 mg of FaSAMS1, protein concentration reached at 0.454 mgÂ·mL-1, the activity of the

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31

Shin, Hye Young, Gi Hoon Kim, Sang Jae Kang, Jeung-Sul Han, and Cheol Choi. "Optimization of Agrobacterium-mediated transformation procedure for grapevine ‘Kyoho’ with carrot antifreeze protein gene." Journal of Plant Biotechnology 44, no. 4 (2017): 388–93. http://dx.doi.org/10.5010/jpb.2017.44.4.388.

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32

Xu, Wen-li, Mei-qin Liu, Xin Shen, and Cun-fu Lu. "Expression of a carrot 36 kD antifreeze protein gene improves cold stress tolerance in transgenic tobacco." Forestry Studies in China 7, no. 4 (2005): 11–15. http://dx.doi.org/10.1007/s11632-005-0039-3.

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33

Cheng, Libao, Xuan Gao, Hussain Javeed, et al. "RETRACTED ARTICLE: Isolation and Functional Characterization of an Antifreeze Protein Gene, TaAFPIII, from Wheat (Triticum aestivum)." Plant Molecular Biology Reporter 30, no. 6 (2012): 1513. http://dx.doi.org/10.1007/s11105-012-0415-9.

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34

Davis, Thomas M., Kevin M. Folta, M. M. Shields, Robin L. Brese, Laura M. R. DiMeglio, and Qian Zhang. "New Genomics Resources for Strawberry." HortScience 40, no. 4 (2005): 1146E—1147. http://dx.doi.org/10.21273/hortsci.40.4.1146e.

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The past year has brought substantial progress in the development of functional and structural genomic tools for strawberry. Sequencing of cDNA library clones from the cultivated strawberry Fragaria × ananassa and the diploid model species Fragaria vesca has provided more than 3000 new EST sequences. We have also constructed a large (∼40 kb) insert genomic (fosmid) library from F. vesca. About 33,000 fosmid clones have been picked and spotted onto hybridization filters. Filters have been successfully probed with three single copy gene probes, one gene family probe, and chloroplast DNA (cpDNA)

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35

Holmberg, Niklas, Judith Farrés, James E. Bailey, and Pauli T. Kallio. "Targeted expression of a synthetic codon optimized gene, encoding the spruce budworm antifreeze protein, leads to accumulation of antifreeze activity in the apoplasts of transgenic tobacco." Gene 275, no. 1 (2001): 115–24. http://dx.doi.org/10.1016/s0378-1119(01)00635-7.

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36

Arai, Tatsuya, Akari Yamauchi, Ai Miura, et al. "Discovery of Hyperactive Antifreeze Protein from Phylogenetically Distant Beetles Questions Its Evolutionary Origin." International Journal of Molecular Sciences 22, no. 7 (2021): 3637. http://dx.doi.org/10.3390/ijms22073637.

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Beetle hyperactive antifreeze protein (AFP) has a unique ability to maintain a supercooling state of its body fluids, however, less is known about its origination. Here, we found that a popular stag beetle Dorcus hopei binodulosus (Dhb) synthesizes at least 6 isoforms of hyperactive AFP (DhbAFP). Cold-acclimated Dhb larvae tolerated −5 °C chilled storage for 24 h and fully recovered after warming, suggesting that DhbAFP facilitates overwintering of this beetle. A DhbAFP isoform (~10 kDa) appeared to consist of 6−8 tandem repeats of a 12-residue consensus sequence (TCTxSxNCxxAx), which exhibite

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37

Sorhannus, Ulf. "Evolution of Antifreeze Protein Genes in the Diatom Genus Fragilariopsis: Evidence for Horizontal Gene Transfer, Gene Duplication and Episodic Diversifying Selection." Evolutionary Bioinformatics 7 (January 2011): EBO.S8321. http://dx.doi.org/10.4137/ebo.s8321.

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38

Liu, Xiangjian, Haiyan Peng, Jingxian Xie, et al. "Methods in Biosynthesis and Characterization of the Antifreeze Protein (AFP) for Potential Blood Cryopreservation." Journal of Nanomaterials 2021 (June 25, 2021): 1–8. http://dx.doi.org/10.1155/2021/9932538.

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The cryopreservation of red blood cells (RBCs) is very important to modern medicine. Cryoprotectants (CPAs) such as dimethyl sulfoxide (DMSO), proline, trehalose, and polyvinyl alcohol (PVA) have been used in the cryopreservation of RBCs, but the results are not satisfactory. Marinomonas primoryensis antifreeze protein (MpAFP) is a Ca2+-dependent AFP derived from Antarctic bacteria, which can prevent bacteria from freezing under extremely cold conditions and may be suitable for cryopreservation of RBCs. The active region of MpAFP is located in region IV and is called MPAFP_RIV. In this paper,

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39

Fan, Y., B. Liu, H. Wang, S. Wang, and J. Wang. "Cloning of an antifreeze protein gene from carrot and its influence on cold tolerance in transgenic tobacco plants." Plant Cell Reports 21, no. 4 (2002): 296–301. http://dx.doi.org/10.1007/s00299-002-0495-3.

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40

Georges, Fawzy, Mohammed Saleem, and Adrian J. Cutler. "Design and cloning of a synthetic gene for the flounder antifreeze protein and its expression in plant cells." Gene 91, no. 2 (1990): 159–65. http://dx.doi.org/10.1016/0378-1119(90)90083-4.

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41

Deng, Long-Qun, Hao-Qiang Yu, Yan-Ping Liu, et al. "Heterologous expression of antifreeze protein gene AnAFP from Ammopiptanthus nanus enhances cold tolerance in Escherichia coli and tobacco." Gene 539, no. 1 (2014): 132–40. http://dx.doi.org/10.1016/j.gene.2014.01.013.

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42

Lazarus, Colin M., and Heather Macdonald. "Characterization of a strawberry gene for auxin-binding protein, and its expression in insect cells." Plant Molecular Biology 31, no. 2 (1996): 267–77. http://dx.doi.org/10.1007/bf00021789.

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43

Goetz, Frederick W., Linda McCauley, Giles W. Goetz, and Birgitta Norberg. "Using global genome approaches to address problems in cod mariculture1." ICES Journal of Marine Science 63, no. 2 (2006): 393–99. http://dx.doi.org/10.1016/j.icesjms.2005.10.006.

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Abstract A number of techniques, including expressed sequence tag (EST) analysis, serial analysis of gene expression, and micro-arrays, are available to study the global expression and regulation of genes. Many of these techniques are being used for intensively reared fish such as trout, salmon, and catfish to study genes involved in growth, reproduction, and health. In contrast, relatively little is known about the composition and regulation of transcriptomes in gadids. However, several bottlenecks in cod mariculture might benefit from the discovery and analysis of genes involved in reproduct

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44

Tzanetakis, I. E., W. M. Wintermantel, and R. R. Martin. "First Report of Beet pseudo yellows virus in Strawberry in the United States: A Second Crinivirus Able to Cause Pallidosis Disease." Plant Disease 87, no. 11 (2003): 1398. http://dx.doi.org/10.1094/pdis.2003.87.11.1398c.

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During efforts to characterize strawberry pallidosis disease, we identified a single strawberry plant that indexed positive for pallidosis disease by grafting but it was not infected with the Strawberry pallidosis associated virus (SPaV) based on reverse transcription-polymerase chain reaction (1). Leaves of this plant were grafted onto Fragaria vesca UC-4 and UC-5 and F. virginiana UC-10 and UC-11 indicator plants. The F. vesca plants remained asymptomatic, while the F. virginiana plants gave typical pallidosis symptoms that included marginal leaf chlorosis and epinasty. The combination of th

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45

Zhang, Yuhua, and Ding S. Shih. "Isolation of an osmotin-like protein gene from strawberry and analysis of the response of this gene to abiotic stresses." Journal of Plant Physiology 164, no. 1 (2007): 68–77. http://dx.doi.org/10.1016/j.jplph.2006.02.002.

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46

Zhang, Geng, Sizhen Jia, Zhiming Yan, Yuanhua Wang, Fengxia Zhao, and Yefan Sun. "A strawberry mitogen-activated protein kinase gene, FaMAPK19, is involved in disease resistance against Botrytis cinerea." Scientia Horticulturae 265 (April 2020): 109259. http://dx.doi.org/10.1016/j.scienta.2020.109259.

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Schaart, Jan G., Lisbeth Mehli, and Henk J. Schouten. "Quantification of allele-specific expression of a gene encoding strawberry polygalacturonase-inhibiting protein (PGIP) using PyrosequencingTM." Plant Journal 41, no. 3 (2004): 493–500. http://dx.doi.org/10.1111/j.1365-313x.2004.02299.x.

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Torrico, A. K., M. G. Celli, E. E. Cafrune, D. S. Kirschbaum, and V. C. Conci. "Genetic variability and recombination analysis of the coat protein gene of Strawberry mild yellow edge virus." Australasian Plant Pathology 45, no. 4 (2016): 401–9. http://dx.doi.org/10.1007/s13313-016-0426-3.

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Leng, Xiangpeng, Dan Liu, Mizhen Zhao, et al. "Genome-wide identification and analysis of FK506-binding protein family gene family in strawberry (Fragaria×ananassa)." Gene 534, no. 2 (2014): 390–99. http://dx.doi.org/10.1016/j.gene.2013.08.056.

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Xiong, Jin-Song, Dan Zheng, Hong-Yu Zhu, Jian-Qiu Chen, Ran Na, and Zong-Ming Cheng. "Genome-wide identification and expression analysis of the SPL gene family in woodland strawberry Fragaria vesca." Genome 61, no. 9 (2018): 675–83. http://dx.doi.org/10.1139/gen-2018-0014.

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Abstract:

SQUAMOSA promoter-binding protein-like (SPL) is a class of plant-specific transcription factors that play critical roles in regulating plant growth and development. However, little systematic research on SPL genes has been conducted in strawberry. In this study, 14 SPL genes were identified in the genome of woodland strawberry (Fragaria vesca), one of the model plants of the family Rosaceae. Chromosome localization analysis indicated that the 14 FvSPL genes were unevenly distributed on six chromosomes. Phylogenetic analysis indicated that the FvSPL proteins could be clustered into six groups (

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