References
- Abe M, Abe K, Kuroda M, Arai S (1992) Corn kernel cysteine proteinases inhibitor as a novel cystatin superfamily member of plant origin. Eur J Biochem 209: 933-937 https://doi.org/10.1111/j.1432-1033.1992.tb17365.x
- Abe K, Emori Y, Kondo H, Suzuki K, Arai S (1987) Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds. J Biol Chem 262: 16793-16797
- Abraham Z, Martinez M, Carbonero P, Diaz I (2006) Structural and functional diversity within the cystatin gene family of Hordeum vulgare. J Exp Bot 57: 4245-4255 https://doi.org/10.1093/jxb/erl200
- Arai S, Matsumoto I, Kondo H, Emori Y, Abe K (2002) Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J Arg Food Chem 50: 6612-6617 https://doi.org/10.1021/jf0201935
- Arai S, Watanabe H, Kondo H, Emori Y, and Abe K (1991) Papain inhibitory activity of oryzacystatin, a rice seed cysteine proteinases inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members. J Biochem 109: 294-298
- Audic S, Claverie JM (1997) The significant digital gene expression profiles. Genome Res 7: 986-995 https://doi.org/10.1101/gr.7.10.986
- Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J, Turk V (1988) The 2.0 Å X-ray crystal structure of chicken egg-white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7: 2593-2599
- Burge CB, Karlin (1998) Finding the genes in genomic DNA. Curr Opin Struc Biol 238: 346-354
- Chirgwin JM, Przybyla AE, MacDonald RJ, Rutter WJ (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochem 18: 5294-5299 https://doi.org/10.1021/bi00591a005
- Flores VMG, Louro RP, Xavier-Filho J, Barratt DHP, Shewry PR. Fernandes KVS (2001) Temporal and tissue localization of a cowpea (Vigna unguiculata) cystatin. Physiol Plant 112: 195-199 https://doi.org/10.1034/j.1399-3054.2001.1120207.x
- Gaddour K, Vicente-Carbajosa J, Lara P, Isabel-Lamoneda I, Diaz I. Carbonero P (2001) A constitutive cystatinencoding gene from barley (Icy) responds differentially to abiotic stimuli. Plant Mol Biol 45: 599-608 https://doi.org/10.1023/A:1010697204686
- Hong JK, Hwang JE, Lim CJ, Yang KA, Jin JL, Kim CY, Koo JC, Chung WS, Lee KO, Lee SY, Cho MJ, Lim CO (2007) Over-expression of Chinese cabbage phytocystatin 1 retards seed germination in Arabidopsis. Plant Sci 172: 556-563 https://doi.org/10.1016/j.plantsci.2006.11.005
- Hong JK, Hwang JE, Lim CJ, Lee KO, Chung WS, Park B-S, Lim CO (2008) Molecular characterization of phytocystatin isolated from Chinese cabbage flower buds. Gene Genomics 30: 235-243
- Kim JS, Chun TY, J.king G, Jin M, Yang TJ, Jin Y-M, Kim H-I, Park B-S (2006) A sequence-tagged linkage map of Brassica rapa. Genetics 174: 29-39 https://doi.org/10.1534/genetics.106.060152
- Kondo H, Abe K, Emori Y, Arai S (1991) Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of animal cystatins. FEBS Lett 278: 87-90 https://doi.org/10.1016/0014-5793(91)80090-P
- Kondo H, Abe K, Nishimure I, Watanabe H, Emori Y, Arai S (1990) Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases: molecular cloning, expression, and biochemical studies on oryzacystatin-II. J Biol Chem 256: 15832-15837
- Kouzuma Y, Inanaga H, Doi-Kawano K, Yamasaki N, Kimura M (2000) Molecular cloning and functional expression of cDNA encoding the cysteine proteinase inhibitor with three cystatin domains from sunflower seeds. J Biochem 128: 161-166 https://doi.org/10.1093/oxfordjournals.jbchem.a022736
- Kumar S, Tamura K, Nei M (2004) MEGA3, integrated software for molecular evolutionary genetic analysis and sequence alignment. Brief Bioinform 5: 150-163 https://doi.org/10.1093/bib/5.2.150
- Kuroda M, Ishimoto M, Suzuki K, Kondo H, Abe K, Kitamura K, Arai S (1996) Oryzacystatins exhibit growth inhibitory and lethal effects on different species of bean insect pests. Callosobruchus chinensis (Coleoptera) and Riptortus calavatus (Hemiptera), Biosci. Biotechnol. Biochem. 60: 209-212 https://doi.org/10.1271/bbb.60.209
- Kuroda M, Kiyosaki T, Matsumoto I, Misaka T, Arai S, Abe K (2001) Molecular cloning, characterization, and expression of wheat cystatins. Biosci Biotechnol Biochem 65: 22-28 https://doi.org/10.1271/bbb.65.22
- Lecardonnel A, Chauvin L, Jouanin L, Beaujean A, Prevost G, Sangwan-Norreel B (1999) Effects of rice cystatin I expression in transgenic potato on Colorado potato beetle larvae. Plant Sci 140: 71-79 https://doi.org/10.1016/S0168-9452(98)00197-6
- Lee SC, Lim MH, Kim JA, Lee SI, Kim JS, Jin M, Kwon SJ, Mun JH, Kim YK, Kim HU, Hur Y, Park BS (2008) Transcriptome analysis in Brassica rapa under the abiotic stresses using Brassica 24K oligo microarray. Mol Cells (in press)
- Lim CO, Kim HY, Kim MG, Lee SI, Chung WS, Park SH, Hwang I, Cho MJ (1996a) Expressed sequence tags of Chinese cabbage flower bud cDNA. Plant Physiol 111: 577-588 https://doi.org/10.1104/pp.111.2.577
- Lim CO, Lee SI, Chung WS, Park SH, Hwang I. Cho MJ (1996b) Characterization of a cDNA encoding cysteine proteinase inhibitor from Chinese cabbage (Brassica campestris L. ssp. pekinensis) flower buds Plant Mol. Biol. 30: 373-379 https://doi.org/10.1007/BF00020124
- Machleidt W, Thiele U, Laber B, Assfalg-Machleidt I, Esterl A, Wiegand G, Kos J, Turk ,V Bode W (1989) Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor. FEBS Lett 243: 234-238 https://doi.org/10.1016/0014-5793(89)80135-8
- Margis R, Reis EM, Villeret V (1998) Structural and phylogenetic relationships among plant and animal cystatins. Arch Biochem Biophys 359: 24-30 https://doi.org/10.1006/abbi.1998.0875
- Martínez M, Abraham Z, Carbonero P, Díaz I (2005) Comparative phylogenetic analysis of cystatin gene families from Arabidopsis, rice and barley. Mol Gen Genomics 273: 423-432 https://doi.org/10.1007/s00438-005-1147-4
- Misaka T, Kuroda M, Iwabuchi K, Abe K. Arai S (1996) Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin. Eur J. Biochem 240: 609-614 https://doi.org/10.1111/j.1432-1033.1996.0609h.x
- Nagata K, Kudo N, Abe K, Arai S, Tanokura M (2000) Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry 39: 14753-14760 https://doi.org/10.1021/bi0006971
- Peitsch M (1996) ProMod and Swiss-Model: internet-based tools for automated comparative protein modeling. Biochem Soc T 224: 274-279
- Pernas M, Sánchez-Monge R, Gómez L, Salcedo G (1998) A chestnut seed cystatin differentially effective against cysteine proteinases from closely related pests. Plant Mol Biol 38: 1235-1242 https://doi.org/10.1023/A:1006154829118
- Sayle R, Milner-White EJ (1995) RasMol: biomolecular graphics for all. Trends Biochem Sci 20: 374 https://doi.org/10.1016/S0968-0004(00)89080-5
- Soares-Costa A, Beltramini LM, Thiemann OH, Henrique-Silva F (2002) A sugarcane cystatin: recombinant expression, purification, and antifungal activity. Biochem Biophys Res Commun 296: 1194-1199 https://doi.org/10.1016/S0006-291X(02)02046-6
- Stubbs MT, Laber B, Bode W, Huber R, Jerala R, Lenarcic B, Turk V (1990) The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J 9: 1939-1947
- Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol Plant 15: 473-497 https://doi.org/10.1111/j.1399-3054.1962.tb08052.x
- Turk B, Krizaj I, Kralj B, Dolenc I, Popovic T, Bieth JG, Turk V (1993) Bovine stefin C, a new member of the stefin family. J Biol Chem 268: 7323-7329
- Turk V, Bode W (1991) The cystatins: Protein inhibitors of cysteine proteinases. FEBS Lett 285: 0231-219
- Vain P, Worland B, Clarke MC, Richard G, Beavis M, Liu H, Kohli A, Leech M, Snape J, Christou P, Atkinson H (1998) Expression of an engineered cysteine proteinase inhibitor (Oryzacystatin-IDELTAD86) for nematode resistance in transgenic rice plants. Theor Appl Genet 96: 266-271 https://doi.org/10.1007/s001220050735
- Yamaguchi-Shinozaki K, Shinozaki K (1994) A novel cis-acting element in Arabidopsis gene is involved in responsiveness to drought, low-temperature, or high-salt stress. Plant cell 6: 251-264 https://doi.org/10.1105/tpc.6.2.251
- Yang KA, Lim CJ, Hong JK, Park CY, Cheong YH, Chung WS, Lee KO, Lee SY, Cho MJ, Lim CO (2006) Identification of cell wall genes modified by a permissive high temperature in Chinese cabbage. Plant Sci 171: 175-182 https://doi.org/10.1016/j.plantsci.2006.03.013
- Yao K, Lockhart KM, Kalanack JJ (2005) Cloning of dehydrin coding sequences from Brassica juncea and Brassica napus and their low temperature-inducible expression in germinating seeds. Plant Physiol Biochem 43: 83-89 https://doi.org/10.1016/j.plaphy.2004.12.006
- Zhao Y, Botella MA, Subramanian L, Niu X, Nielsen SS, Bressan RA, Hasegawa PM (1996) Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol 111: 1299-1306 https://doi.org/10.1104/pp.111.4.1299
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