PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2011 | 33 | 6 |
Tytuł artykułu

Biochemical characterization of the Arabidopsis KS-type dehydrin protein, whose gene expression is constitutively abundant rather than stress dependent

Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Dehydrins are known as plant stress-responsive genes. Arabidopsis thaliana has 10 dehydrin genes. Among them, one of the highly expressed genes is a KS-type dehydrin (At1g54410). However, the gene product, which is a histidine-rich dehydrin whose molecular mass is 11 kDa (AtHIRD11), has not been studied. Thus, we report the biochemical characterization of the AtHIRD11 protein. Although the AtHIRD11 protein was detected in all organs of Arabidopsis, the bolting stem and the flower showed higher accumulation than the other organs, with the AtHIRD11 protein detected in the cambial zone of the stem vasculature. Most of the AtHIRD11 protein was found to be a bound form. The bound AtHIRD11 was solubilized by 1 M NaCl solution. The extracted AtHIRD11 was retained in immobilized metal-affinity chromatography, and eluted by an imidazole gradient. The native AtHIRD11 prepared from Arabidopsis was partially phosphorylated, but further phosphorylated by casein kinase 2 in vitro. Metal-binding assays indicated that Zn²⁺ may be the best metal for AtHIRD11 binding. These results suggest that AtHIRD11 is a metal-binding dehydrin that shows a house-keeping expression in Arabidopsis.
Słowa kluczowe
Wydawca
-
Rocznik
Tom
33
Numer
6
Opis fizyczny
Twórcy
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizouka 422-8529, Japan
autor
  • Division of Global Research Leaders, Shizuoka Unversity, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan
Bibliografia
  • Abu-Abied M, Golomb L, Belausov E, Huang S, Geiger B, Kam Z, Staiger CJ, Sadot E (2006) Identification of plant cytoskeletoninteracting proteins by screening for actin stress fiber association in mammalian fibroblasts. Plant J 48:367–379
  • Alsheikh MK, Heyen BJ, Randall SK (2003) Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation. J Biol Chem 278:40882–40889
  • Alsheikh MK, Svensson JT, Randall SK (2005) Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins. Plant Cell Environ 28:1114–1122
  • Battaglia M, Olvera-Carrillo Y, Garciarrubio A, Campos F, Covarrubias AA (2008) The enigmatic LEA proteins and other hydrophilins. Plant Physiol 148:6–24
  • Bravo LA, Close TJ, Corcuera LJ, Guy CL (1999) Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation. Physiol Plant 106:177–183
  • Brini F, Hanin M, Lumbreras V, Amara I, Khoudi H, Hassairi A, Pagès M, Masmoudi K (2007) Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana. Plant Cell Rep 26:2017–2026
  • Cheng Z, Targolli J, Huang X, Wu R (2002) Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.). Mol Breed 10:71–82
  • Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97:795–803
  • Danyluk J, Perron A, Houde M, Limin A, Fowler B, Benhamou N, Sarhan F (1998) Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat. Plant Cell 10:623–638
  • Figueras M, Pujal J, Saleh A, Save R, Pagès M, Goday A (2004) Maize Rabl7 overexpression in Arabidopsis plants promotes osmotic stress tolerance. Ann Appl Biol 144:251–257
  • Godoy JA, Lunar R, Torres-Schumann S, Moreno J, Rodrigo RM, Pintor-Toro JA (1994) Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants. Plant Mol Biol 26:1921–1934
  • Hara M (2010) The multifunctionality of dehydrins: an overview. Plant Signal Behav 5:503–508
  • Hara M, Terashima S, Fukaya T, Kuboi T (2003) Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco. Planta 217:290–298
  • Hara M, Fujinaga M, Kuboi T (2005) Metal binding by citrus dehydrin with histidine-rich domains. J Exp Bot 56:2695–2703
  • Hara M, Shinoda Y, Tanaka Y, Kuboi T (2009) DNA binding of citrus dehydrin promoted by zinc ion. Plant Cell Environ 32:532–541
  • Heyen BJ, Alsheikh MK, Smith EA, Torvik CF, Seals DF, Randall SK (2002) The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation. Plant Physiol 130:675–687
  • Hirayama T, Shinozaki K (2010) Research on plant abiotic stress responses in the post-genome era: past, present and future. Plant J 61:1041–1052
  • Houde M, Dallaire S, N’Dong D, Sarhan F (2004) Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves. Plant Biotechnol J 2:381–387
  • Hundertmark M, Hincha DK (2008) LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 9:118
  • Ismail AM, Hall AE, Close TJ (1999) Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence. Proc Natl Acad Sci USA 96:13566–13570
  • Jiang X, Wang Y (2004) β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein. Biochemistry 43:15567–15576
  • Koag MC, Wilkens S, Fenton RD, Resnik J, Vo E, Close TJ (2009) The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant Physiol 150:1503–1514
  • Kovacs D, Kalmar E, Torok Z, Tompa P (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol 147:381–390
  • Krüger C, Berkowitz O, Stephan UW, Hell R (2002) A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L. J Biol Chem 277:25062–25069
  • Nylander M, Svensson J, Palva ET, Welin BV (2001) Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana. Plant Mol Biol 45:263–279
  • Plana M, Itarte E, Eritja R, Goday A, Pages M, Martinez MC (1991) Phosphorylation of the maize RAB-17 protein by casein kinase 2. J Biol Chem 266:22510–22514
  • Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET (2004) Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis. Plant Mol Biol 54:743–753
  • Reyes JL, Campos F, Wei H, Arora R, Yang Y, Karlson DT, Covarrubias AA (2008) Functional dissection of hydrophilins during in vitro freeze protection. Plant Cell Environ 31:1781–1790
  • Röhrig H, Schmidt J, Colby T, Bräutigam A, Hufnagel P, Böhm N, Bartels D (2006) Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation. Plant Cell Environ 29:1606–1615
  • Rorat T (2006) Plant dehydrins: tissue location, structure and function. Cell Mol Biol Lett 11:536–556
  • Rorat T, Grygorowicz WJ, Irzykowski W, Rey P (2004) Expression of KS-type dehydrins is primarily regulated by factors related to organ type and leaf developmental stage during vegetative growth. Planta 218:878–885
  • Skirycz A, Inzé D (2010) More from less: plant growth under limited water. Curr Opin Biotechnol 21:197–203
  • Svensson J, Palva ET, Welin B (2000) Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expr Purif 20:169–178
  • Svensson J, Ismail AM, Palva ET, Close TJ (2002) Dehydrins. In: Storey KB, Storey JM (eds) Sensing. Signaling and cell adaptation, Elsevier, pp 155–171
  • Tompa P (2009) Structure and function of intrinsically disordered proteins. CRC Press, FL
  • Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K (2006) Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 91:2243–2249
  • Tunnacliffe A, Wise MJ (2007) The continuing conundrum of the LEA proteins. Naturwissenschaften 94:791–812
  • Ueda EKM, Gout PW, Morganti L (2003) Current and prospective applications of metal ion-protein binding. J Chromatogr A 988:1–23
  • Wisniewski M, Webb R, Balsamo R, Close TJ, Yu XM, Griffith M (1999) Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica). Physiol Plant 105:600–608
  • Yin Z, Rorat T, Szabala BM, Ziólkowska A, Malepszy S (2006) Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings. Plant Sci 170:1164–1172
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-4988f588-4e70-4a6b-afee-cd0e0cc68061
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.