Ribozom İnaktive Eden Proteinlerin Bitki Virüs Hastalıklarının Kontrolünde Kullanılma Olanakları

Nihan Güneş, Hikmet Murat Sipahioğlu, Mustafa Gümüş

Abstract


Ribozom inaktive eden proteinler (RIP’ler) olarak adlandırılan bir grup protein, enzimatik yolla geri dönülmez bir şekilde ribozomlara zarar verme yeteneğindedir. RIP’ler Cucurbitaceae, Euphorbiaceae, Poaceae ve Caryophyllaceae gibi familyalara ait bazı bitki türlerinde yaygın olarak bulunmakla beraber bazı fungus ve deniz yosunlarında da saptanmıştır. RIP’ler genel olarak moleküler yapısına göre Tip1, Tip2 ve Tip3 olmak üzere 3 grupta toplanmaktadır. Doğadaki rolleri henüz tam olarak anlaşılmamış olmakla beraber, bazı özelliklerinin ortaya koyulması tarımsal uygulamalarda onlardan faydalanmak konusunda umut verici olmuştur. Bu proteinlerin bitkiler için patojenik olan bazı fungus ve virüslere karşı etkili olduğu çeşitli çalışmalarda rapor edilmiştir. Yapı, fonksiyon ve biyolojik aktiviteleri göz önüne alındığında bitkilerden izole edilen RIP’lerin gösterdikleri antiviral aktivitenin bitki virüs hastalıklarıyla mücadelede yeni gelişmeler açısından potansiyel taşıdığı görülmektedir.

Keywords


Ribozom inaktive eden proteinler (RIP) Antiviral aktivite Bitki virüs hastalıkları

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References


Balasaraswathi R, Sadasivam S, Ward M and Walker JM (1998). An antiviral protein from Bougainvillea spectabilis roots; purification and characterisation, Phytochemistry, 47(8):1561-1565 pp.

Balasubrahmanyam A, Baranwal VK, Lodha ML, Varma A and Kapoor HC (2000). Purification and properties of growth stage-dependent antiviral pro-teins from the leaves of Celosia cristata, Plant sci-ence, 154(1):13-21 pp.

Baranwal, VK, Turner NE and Kapoor HC (2002). Depurination of ribosomal RNA and inhibition of viral RNA translation by an antiviral protein of Ce-losia cristata, Indian Journal of Experimental Bio-logy, 40:1195-1197 pp.

Barbieri L, Valbonesi P, Bondioli M, Lugo Alvarez M, Dal Monte P, Landini MP and Stirpe F (2001). A-denine glycosylase activity in mammalian tissues: an equivalent of ribosomeinactivating proteins. FEBS Letters, 505, 196–197 pp.

Barbieri L, Brigotti M, Perocco P, Carnicelli D, Ciani M, Mercatali L and Stirpe F (2003). Ribosome‐inactivating proteins depurinate poly (ADP‐ribosyl) ated poly (ADP‐ribose) polymerase and have trans-forming activity for 3T3 fibroblasts. FEBS letters, 538(1-3):178-182 pp.

Begam M, Kumar S, Roy S, Campanella JJ and Ka-poor HC (2006). Molecular cloning and functional identification of a ribosome inactivating/antiviral protein from leaves of post-flowering stage of Celo-sia cristata and its expression in E. coli, Phytoche-mistry, 67(22):2441-2449 pp.

Bhatia S and Lodha ML (2005). RNase and DNase activities of antiviral proteins from leaves of Bou-gainvillea xbuttiana, Indian Journal of Bioche-mistry and Biophysics, 42:152–155 pp.

Chaudhry B, Müller‐Uri F, Cameron‐Mills V, Gough S, Simpson D, Skriver K and Mundy J (1994). The barley 60 kDa jasmonate‐induced protein (JIP60) is a novel ribosome‐inactivating protein. The Plant Journal, 6(6):815-824 pp.

Chen ZC, White RF, Antoniw JF and Lin Q (1991). Effect of pokeweed antiviral protein (PAP) on the infection of plant viruses, Plant Pathology, 40(4):612-620 pp.

Chen Y, Peumans WJ and Van Damme EJ (2002). The Sambucus nigra type‐2 ribosome‐inactivating pro-tein SNA‐I′ exhibits in planta antiviral activity in transgenic tobacco, FEBS letters, 516(1-3):27-30 pp.

Choudhary NL, Yadav, OP and Lodha ML (2008a). Ribonuclease, deoxyribonuclease, and antiviral ac-tivity of Escherichia coli-expressed Bougainvillea xbuttiana antiviral protein1, Biochemistry, 73(3):273-277 pp.

Choudhary N, Kapoor HC and Lodha ML (2008b). Cloning and expression of antiviral/ribosome-inactivating protein from Bougainvillea xbuttiana, Journal of biosciences, 33(1).

de Benito, FM. Citores L, Iglesias R, Ferreras JM, Sori-ano F, Arias FJ, Me´ndez E and Girbe´s T (1995). Ebulitins: a new family of type 1 ribosome-inactivating proteins (rRNA Nglycosidases) from leaves of Sambucus ebulus L. that coexist with the type 2 ribosome-inactivating protein ebulin l, FEBS Letters, 360:299-302 pp.

Endo Y, Mitsui K, Motizuki M and Tsurugi K (1987). The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S riboso-mal RNA caused by the toxins, Journal of Biologi-cal Chemistry, 262(12):5908–5912 pp.

Ferreras JM, Barbieri L, Girbés T, Battelli MG, Rojo, M.A., Arias, F.J., Rocher, M.A., Soriano, F., Men-de´z, E. and Stirpe, F (1993). Distribution and pro-perties of major ribosome-inactivating proteins (28 S rRNA N-glycosidases) of the plant Saponaria officinalis L. (Caryophyllaceae), Biochimica et Bi-ophysica Acta (BBA)-Gene Structure and Expressi-on, 1216:31–42 pp.

Girbés T, Ferreras JM, Arias FJ, Mun˜oz R, Iglesias R, Jime´nez P, Rojo MA, Arias Y, Perez Y, Benitez J, Sanchez D and Gayoso MJ (2003). Non-toxic type 2 ribosomeinactivating proteins (RIPs) from Sam-bucus: occurrence, cellular and molecular activities and potential uses, Cellular and molecular biology (Noisy-le-Grand, France), 49:537–545 pp.

Girbés T, Ferreras JM, Arias FJ and Stirpe F (2004). Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria, Mini reviews in medi-cinal chemistry, 4(5):461-476 pp.

Guo YJ, Demin J, Man Li W, Guo B, Bin W, Jin DM, Weng ML, Guo B and Wang B (1999). Transfor-maton and expression of trichosanthin gene in to-mato, Acta Botanica Sinica, 41:334–336 pp.

Güller A (2015). Begonvil (Bougainvillea spectabilis willd.) bitkisindeki boganin protein geninin klon-lanması, bakteriyel ekspresyonu, antiviral ve anti-mikrobiyal aktivitesinin araştırılması, Doktora Te-zi, Yüzüncü Yıl Üniversitesi Fen Bilimleri Enstitüsü Biyoloji Anabilim Dalı, 107s.

Hao Q, Van Damme EJ, Hause B, Barre A, Chen Y, Rouge´ P, Peumans WJ (2001). Iris bulbs express type 1 and type 2 ribosome-inactivating proteins with unusual properties, Plant physiology, 125:866-876 pp.

Hartley MR, Legname G, Osborn R, Chen Z and Lord J.M (1991). Single chain ribosome inactivating pro-teins from plants depurinate Escherichia coli 23S ribosomal RNA, FEBS letters, 290(1-2):65-68 pp.

Hong Y, Saunders K, Hartley MR and Stanley J (1996). Resistance to geminivirus infection by vi-rus-induced expression of dianthin in transgenic plants, Virology, 220(1):119-127 pp.

Kubo S, Ikeda T, Imaizumi Y and Mikami Y (1990). A potent plant virus inhibitor found in Mirabilis jala-pa L., Japanese Journal of Phytopathology, 56:481-487 pp.

Lam SK and Ng TB (2001). First simultaneous isolati-on of a ribosome inactivating protein and an anti-fungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects. Archives of Biochemistry and Biophysics, 393(2), 271-280 pp.

Li Y, Jia Y, Zhang Z, Chen X, He H, Fang R and Hao X (2007). Purification and Characterization of a New Ribosome Inactivating Protein from Cinchonagly-coside C‐treated Tobacco Leaves, Journal of In-tegrative Plant Biology, 49(9):1327-1333 pp.

Liu RS, Yang JH and Liu WY (2002). Isolation and enzymatic characterization of lamjapin, the first ri-bosome-inactivating protein from cryptogamic al-gal plant (Laminaria japonica A), The FEBS Jour-nal, 269, 4746–4752 pp.

Lodge JK, Kaniewski WK and Tumer NE (1993). Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein, Pro-ceedings of the National Academy of Sciences, 90(15):7089-7093 pp.

Park SW, Stevens NM and Vivanco JM (2002). En-zymatic specificity of three ribosome-inactivating proteins against fungal ribosomes, and correlation with antifungal activity, Planta, 216(2):227-234 pp.

Picard D, Kao CC and Hudak KA (2005). Pokeweed antiviral protein inhibits brome mosaic virus repli-cation in plant cells, Journal of Biological Che-mistry, 280(20):20069-20075 pp.

Roy S, Sadhana P, Begum M, Kumar S, Lodha ML and Kapoor HC (2006). Purification, characteriza-tion and cloning of antiviral/ribosome inactivating protein from Amaranthus tricolor leaves, Phyto-chemistry, 67(17):1865-1873 pp.

Sipahioğlu HM, Kaya HM, Usta M, Ünal M, Özcan D, Özer M, Güller A, and Pallas, V (2017). Pokeweed (Phytolacca americana L.) antiviral protein inhibits Zucchini yellow mosaic virus infection in a dose-dependent manner in squash plants, Turkish Jour-nal of Agriculture and Forestry, 41:256-262 pp.

Stirpe F, Williams DG, Onyon LJ, Legg RF and Stevens WA (1981). Dianthins, ribosome-damaging proteins with anti-viral properties from Dianthus caryophyl-lus L. (carnation), Biochemical journal, 195(2):399-405 pp.

Stirpe F (2004). Ribosome-inactivating proteins. Toxi-con, 44(4), 371-383.

Stirpe F (2013). Ribosome-inactivating proteins: from toxins to useful proteins. Toxicon, 67, 12-16 pp.

Zhu F, Yuan S, Zhang ZW, Qian K, Feng JG and Yang YZ (2016). Pokeweed antiviral protein (PAP) incre-ases plant systemic resistance to Tobacco mosaic virus infection in Nicotiana benthamiana, Euro-pean Journal of Plant Pathology, 146(3):541-549 pp.

Walsh TA, Morgan AE and Hey TD (1991). Characte-rization and molecular cloning of a proenzyme form of a ribosomeinactivating protein from mai-ze-novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment, Journal of Biological Chemistry,




DOI: https://doi.org/10.15316/SJAFS.2018.141

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