Genotype differences in drought tolerance of photosynthetic apparatus in Festuca arundinacea SCHREB. are connected with Cu-Zn SOD protein accumulation

• Autorzy: Pawlowicz I. , Rapacz M.

Warianty tytułu

PL

Różnice genotypowe w tolerancji aparatu fotosyntetycznego na suszę są u roślin Festuca arundinacea SCHREB. związane z akumulacją białka Cu-Zn SOD

• Języki publikacji: EN

Abstrakty

EN

Festuca arundinacea (Fa) is one of the most drought-tolerant species within the Lolium-Festuca complex. In the current work the protein level of chloroplastic Cu-Zn SOD (superoxide dismutase) in two Fa plants with extreme values of drought tolerance during exposition to water deficit was investigated. The obtain results revealed higher level of enzyme accumulation in more drought-tolerant Fa genotype. In less-drought tolerant plant the increase of dismutase level during stress treatment was only slight.

PL

Festuca arundinacea (Fa) jest jednym z najbardziej odpornych na suszę gatunków w obrębie kompleksu Lolium-Festuca. W niniejszej pracy badano wpływ deficytu wodnego na poziom białka Cu-Zn SOD (dysmutaza ponadtlenkowa) u dwóch genotypów Fa charakteryzujących się skrajnymi wartościami tolerancji na suszę. Wysoką akumulację enzymu podczas stresu obserwowano u rośliny bardziej odpornej na suszę, podczas gdy u rośliny mniej odpornej wzrost poziomu dysmutazy był jedynie nieznaczny.

Słowa kluczowe

EN

genotype difference; drought tolerance; photosynthetic apparatus; Festuca arundinacea; protein level; water deficit; Lolium-Festuca complex; superoxide dismutase

• Wydawca: -
• Czasopismo: Zeszyty Problemowe Postępów Nauk Rolniczych
• Rocznik: 2010
• Tom: 545
• Opis fizyczny: p.191-197,fig.,ref.

Twórcy

autor

Pawlowicz I.

• Institute of Plant Genetics, Polish Academy of Sciences, Strzeszynska 34, 60-479 Poznan, Poland

autor

Rapacz M.

Bibliografia

• Alscher R.G., Erturk N., Lenwood S.H. 2002. Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. J. Exp. Bot. 53: 1331-1341.
• Bradford M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 48-254.
• Clark A.J., Landolt W., Bucher J.B., Strasser R.J. 2000. Beech (Fagus sylvatica) response to ozone exposure assessed with a chlorophyll а fluorescence performance index. Environ. Pollut. 109: 501-507.
• Foyer C.H., Noctor G. 2003. Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria. Physiol. Plant. 119: 355-364.
• Foyer C.H., Noctor G. 2005. Redox homeostis and antioxidant signaling: A metabolic interface between stress perception and physiological responses. Plant Cell 17: 1866-1875.
• Grun S., Lindermayer C., Sell S. 2006. Nitric oxide and gene regulation in plants. J. Exp. Bot. 57: 507-516.
• Gupta A.S., Webb R.P., Holaday A.S., Allen R.D. 1993. Overexpression of superoxide dismutase protects plants from oxidative stress (induction of ascorbate peroxidase in superoxide dismutase-overexpressing plants). Plant Physiol. 103: 1067-1073.
• Hurkman W.J., Tanaka C.K. 1986. Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis. Plant Physiol. 81: 802-806.
• Kamińska-Rożek E., Pukacki P.M. 2004. Ejfect of water deficit on oxidative stress and degradation of cell membranes in needles of Norway spruce (Picea bies). APP 26: 431-442.
• Kanematsu S., Asada K. 1990. Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail. Plant Cell Physiol. 31: 99-112.
• Lee B.H. 2007. Simultaneous overexpression of both CuZn superoxide dismutase and ascorbate peroxidase in transgenic tall fescue plants confers increased tolerance to a wide range of abiotic stresses. J. Plant Physiol. 164: 1626-1638.
• Ogawa K., Kanematsu S., Asada K. 1996. Intra- and extra-cellular localization of „cytosolic” CuZn-superoxide dismutase in spinach leaf and hypocotyl. Plant Cell Physiol. 37: 790-799.
• Oukarroum A., El Madidi S., Schansker G., Strasser R.J. 2007. Probing the responses of barley cultivars (Hordeum vulgare) by chlorophyll a fluorescence OLKJIP under drought stress and re-watering. Environ. Exp. Bot. 60: 438-446.
• Rapacz M. 2007. Chlorophyll a fluorescence transient during freezing and recovery in winter wheat. Photosynthetica 45: 409-418.
• Rapacz M., Kościelniak J., Jurczyk B., Adamska A., Wójcik M. 2009. Different pattems of physiological and molecular response to drought in seedlings of malt- and feed-type barleys (Hordeum vulgare) J. Agron. Crop. Sci. doi: doi:10.1111/j.l439-037X.2009.00389.X.
• Schützendübel A., Polle A. 2002. Plant responses to abiotic stresses: heavy metal-induced oxidative stress and protection by mycorrhization. J. Exp. Bot. 53: 1351-1365.
• Strasser R.J., Tsimilli-Michael M. 2001. Stress in plants, from daily rhythm to global changes, detected and quantified by the JIP-Test. Chem. Nouv. 75: 3321-3326.
• Takahashi M.A., Asada K. 1983. Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch. Biochem. Biophys. 15: 558-566.
• Thomas H., Humphreys M.O. 1991. Progress and potential of interspecific hybrids of Lolium and Festuca. J. Agric. Sci. 117: 1-8.