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Expression pattern of low-temperature-related genes by the treatment of AFP in the cryopreservation of potato shoot tips

감자 정아 동결보존과정에서 AFP 처리 시 저온관련 유전자의 발현양상

  • Seo, Ji-Hyang (Department of Horticulture, Kyungpook National University) ;
  • Jeon, Su Min (Department of Horticulture, Kyungpook National University) ;
  • Naing, Aung Htay (Department of Horticulture, Kyungpook National University) ;
  • Han, Jeung Sul (Department of Horticulture, Kyungpook National University) ;
  • Park, In Hwan (Department of Landscape Architecture, Kyungpook National University) ;
  • Kim, Chang-Kil (Department of Horticulture, Kyungpook National University)
  • Received : 2017.12.11
  • Accepted : 2017.12.18
  • Published : 2017.12.31

Abstract

The expression profiles of low-temperature-related genes were examined in in vitro potatoes exposed to a cold condition for 1-3 days. The expression levels of PPI1 and CI21B genes were lineraly elevated from day 1 to day 3, while the opposite trend was observed for CBF4 and CI21A. In addition, the expression of the genes CI21A and CI21B varied, along with specific tissues (leaf, stem, and tuber) and the treatment periods. Therefore, potato shoot tips were cryopreserved with LS and PVS2 containing different oncentrations of AFP. It can thus be inferred that the presence of AFP in LS and PVS2 was likely to elevate expression pattern of the genes. Furthermore, the concentration of AFP (1,500 ng/ml for LS and 500 ng/mg for PVS2) was the best for the cryopreservation of potatoes.

기내배양한 감자에 1일, 2일, 3일간 저온처리 후 저온관련 유전자의 발현양상을 조사하였다. 저온 처리 기간이 늘어날수록 PPI1, CI21B유전자의 발현양은 증가하였고, CBF4, CI21A 유전자의 발현양은 감소하였다. 또한 CI21A와 CI21B유전자의 잎, 줄기, 괴경에서 명 처리와 암 처리 기간별로 저온 처리기간에 따른 유전자의 발현의 차이를 보았다. 이에 근거하여 감자 정아의 동결과정 중에서 LS단계와 PVS2 단계에서 AFP를 농도별로 처리하였다. 그 결과, 저온처리 기간이 늘었을 때의 유전자 발현양상과 AFP 특정 농도에서의 발현 양상이 동일하였다. LS단계에서는 1,500 ng/ml AFP 처리와, PVS2단계에서 500 ng/ml AFP 처리가 감자 정아의 초저온동결보존에 효과적이라는 것을 유전자의 발현 양상으로 확인하였다.

Keywords

References

  1. Arav A, Rubinsky B, Fletcher G, Seren E (1993) Cryogenic protection of oocytes with antifreeze proteins. Molecular reproduction and development 36:488-493 https://doi.org/10.1002/mrd.1080360413
  2. Atici O, Nalbantoglu B (2003) Antifreeze proteins in higher plants. Phytochemistry 64:1187-1196 https://doi.org/10.1016/S0031-9422(03)00420-5
  3. Carvallo MA, Pino M-T, Jeknic Z, Zou C, Doherty CJ, Shiu S-H, Chen TH, Thomashow MF (2011) A comparison of the low temperature transcriptomes and CBF regulons of three plant species that differ in freezing tolerance: Solanum commersonii, Solanum tuberosum, and Arabidopsis thaliana. Journal of experimental botany 62:3807-3819 https://doi.org/10.1093/jxb/err066
  4. D'Amico S, Collins T, Marx JC, Feller G, Gerday C (2006) Psychrophilic microorganisms: challenges for life. EMBO reports 7:385-389 https://doi.org/10.1038/sj.embor.7400662
  5. Davies PL, Baardsnes J, Kuiper MJ, Walker VK (2002) Structure and function of antifreeze proteins. Philosophical Transactions of the Royal Society of London B: Biological Sciences 357:927-935 https://doi.org/10.1098/rstb.2002.1081
  6. Davies PL, Sykes BD (1997) Antifreeze proteins. Current opinion in structural biology 7:828-834 https://doi.org/10.1016/S0959-440X(97)80154-6
  7. Ekins S, Murray G, Hawksworth G (1996) ULTRASTRUCTURAL AND METABOLIC EFFECTS AFTER VITRIFICATION OF PRECISION-CUTRAT LIVER SLICES WITH ANTIFREEZE PROTEINS. Cryo-letters 17:157-164
  8. Finkle B, Zavala M, Ulrich J (1985) Cryoprotective compounds in the viable freezing of plant tissues. AGRIS
  9. Fletcher GL, Hew CL, Davies PL (2001) Antifreeze proteins of teleost fishes. Annual review of physiology 63:359-390 https://doi.org/10.1146/annurev.physiol.63.1.359
  10. Garcia MNM, Pais SM, Tellez-Inon MT, Capiati DA (2011) Characterization of StPPI1, a proton pump interactor from Solanum tuberosum L. that is up-regulated during tuber development and by abiotic stress. Planta 233:661-674 https://doi.org/10.1007/s00425-010-1329-0
  11. Haake V, Cook D, Riechmann J, Pineda O, Thomashow MF, Zhang JZ (2002) Transcription factor CBF4 is a regulator of drought adaptation in Arabidopsis. Plant physiology 130:639-648 https://doi.org/10.1104/pp.006478
  12. Jeon SM, Naing AH, Park KI, Kim CK (2015) The effect of antifreeze protein on the cryopreservation of chrysanthemums. Plant Cell, Tissue and Organ Culture (PCTOC) 123:665-671 https://doi.org/10.1007/s11240-015-0852-x
  13. Jo JW, Jee BC, Suh CS, Kim SH (2012) The beneficial effects of antifreeze proteins in the vitrification of immature mouse oocytes. PLoS One 7:e37043 https://doi.org/10.1371/journal.pone.0037043
  14. Karimi M, Ebadi A, Mousavi SA, Salami SA, Zarei A (2015) Comparison of CBF1, CBF2, CBF3 and CBF4 expression in some grapevine cultivars and species under cold stress. Scientia horticulturae 197:521-526 https://doi.org/10.1016/j.scienta.2015.10.011
  15. Lee Y-J, Jeong J-C, Yoon Y-H, Hong S-Y, Kim S-J, Jin Y-I, Nam J-H, Kwon O-K (2012) Evaluation of Quality Characteristics and Definition of Utilization Category in Korean Potato (Solanum tuberosum L.) Cultivars. Korean Journal of Crop Science 57:271-279 https://doi.org/10.7740/kjcs.2012.57.3.271
  16. Lizarraga R, Huaman Z, Dodds JH (1989) In vitro conservation of potato germplasm at the International Potato Center. American Journal of Potato Research 66:253-269 https://doi.org/10.1007/BF02853449
  17. Madura JD, Baran K, Wierzbicki A (2000) Molecular recognition and binding of thermal hysteresis proteins to ice. Journal of Molecular Recognition 13:101-113 https://doi.org/10.1002/(SICI)1099-1352(200003/04)13:2<101::AID-JMR493>3.0.CO;2-9
  18. Murashige T, Skoog F (1962) A revised medium for rapid growth and bio assays with tobacco tissue cultures. Physiologia Plantarum 15:473-49722 https://doi.org/10.1111/j.1399-3054.1962.tb08052.x
  19. Mustafa RM, Abeer MA, James G,Song JY, Benildo GR (2005) The OsLti6 genes encoding low-molecular-weight membrane proteins are differentially expressed in rice cultivars with contrasting sensitivity to low temperature. Gene 344:171-180 https://doi.org/10.1016/j.gene.2004.09.033
  20. Nicot N, Hausman J-F, Hoffmann L, Evers D (2005) Housekeeping gene selection for real-time RT-PCR normalization in potato during biotic and abiotic stress. Journal of experimental botany 56:2907-2914 https://doi.org/10.1093/jxb/eri285
  21. Pertaya N, Marshall CB, Celik Y, Davies PL, Braslavsky I (2008) Direct visualization of spruce budworm antifreeze protein interacting with ice crystals: basal plane affinity confers hyperactivity. Biophysical journal 95:333-341 https://doi.org/10.1529/biophysj.107.125328
  22. Sakai A, Kobayashi S, Oiyama I (1990) Cryopreservation of nucellar cells of navel orange (Citrus sinensis Osb. var. brasiliensis Tanaka) by vitrification. Plant Cell Reports 9:30-33
  23. Schneider A, Salamini F, Gebhardt C (1997) Expression patterns and promoter activity of the cold-regulated gene ci21A of potato. Plant physiology 113:335-345 https://doi.org/10.1104/pp.113.2.335
  24. Seo H-W, Yi J-Y, Park Y-E, Cho J-H, Hahm Y-I, Cho H-M (2005) Cloning of coat protein gene from Korean isolate potato leafroll virus (PLRV) and introduction into potato (Solanum tuberosum). Journal of Plant Biotechnology 32:243-250 https://doi.org/10.5010/JPB.2005.32.4.243
  25. Steponkus PL (1985) Cryobiology of isolated protoplasts: applications to plant cell cryopreservation. Cryopreservation of plant cells and organs CRC Press, Boca Raton:49-60
  26. Stushnoff C (1985) The potential use of in vitro storage for temperate fruit germ-plasm: a status report. In, IBPGR
  27. Wang J, Bian H, Zhang Y, Cheng H (2000) The dual effect of antifreeze protein on cryopreservation of rice (Oryza sativa l.) embryogenic suspension cells. Cryo letters 22:175-182
  28. Withers LA (1985) Cryopreservation of cultured cells and meristems. Cell culture and somatic cell genetics of plants 2:253-316
  29. Xiao H, Tattersall EA, Siddiqua MK, Cramer GR, Nassuth A (2008) CBF4 is a unique member of the CBF transcription factor family of Vitis vinifera and Vitis riparia. Plant, cell & environment 31:1-10
  30. Yeh Y, Feeney RE (1996) Antifreeze proteins: structures and mechanisms of function. Chemical Reviews 96:601-618 https://doi.org/10.1021/cr950260c