α-淀粉酶,基因结构,进化,表达," /> α-淀粉酶,基因结构,进化,表达,"/> α-amylase,Gene Structure,Evolution,Expression profiling,"/>
作物学报 ›› 2010, Vol. 36 ›› Issue (1): 17-27.doi: 10.3724/SP.J.1006.2010.00017
廖登群1,2,张洪亮1,李自超1,John BENNETT 2,3
LIAO Deng-Qun1,2,ZHANG Hong-Liang1,LI Zi-Chao1,*,John BENNETT 2,3
摘要:
| [1] Stanley D, Farnden K J F, MacRae E A. Plant α-amylases: functions and roles in carbohydrate metabolism. Biologia, Bratislava, 2005, 60(suppl 16): 65-71 [2] Smith A M, Zeeman S C, Smith S M. Starch degradation. Annu Rev Plant Biol, 2005, 56: 73-98 [3] Beck E, Ziegler P. Biosynthesis and degradation of starch in higher plants. Annu Rev Plant Physiol Plant Mol Biol, 1989, 40: 95-117 [4] Williamson J F, Peterson M L. Relation between alpha amylase activity and growth of rice seedlings. Crop Sci, 1973, 13: 612-614 [5] Karrer E E, Chandler J M, Foolad M R, Rodriguez R L. Correlation between a-amylase gene expression and seedling vigor in rice. Euphytica, 1993, 66: 163-169 [6] Guglielminetti L, Yamaguchi J, Perata P, Alpi A. Amylolytic activities in cereal seeds under aerobic and anaerobic conditions. Plant Physiol, 1995, 109: 1069-1076 [7] Hwang Y S, Thomas B R, Rodriguez R L. Differential expression of rice a-amylase genes during seedling development under anoxia. Plant Mol Biol, 1999, 40: 911-920 [8] Rogers J C. Two barley alpha-amylase gene families are regulated differently in aleurone cells. J Biol Chem, 1985, 260: 3731-3738 [9] Khursheed B, Rogers J C. Barley alpha-amylase genes. Quantitative comparison of steady-state mRNA levels from individual members of the two different families expressed in aleurone cells. J Biol Chem, 1988, 263: 18953-18960 [10] Gubler F, Jacobsen J V. Gibberellin-responsive elements in the promoter of a barley high-pl [alpha]-amylase gene. Plant Cell, 1992, 4: 1435-1441 [11] Sogaard M, Kadziola A, Haser R, Svensson B. Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1. J Biol Chem, 1993, 268: 22480-22484 [12] Huang N, Sutliff T D, Litts J C, Rodriguez R L. Classification and characterization of the rice alpha-amylase multigene family. Plant Mol Biol, 1990, 14: 655-668 [13] Huang N, Koizumi N, Reinl S, Rodriguez R L. Structural organization and differential expression of rice alpha-amylase genes. Nucl Acids Res, 1990, 18: 7007-7014 [14] Ranjhan S, Litts J C, Foolad M R, Rodriguez R L. Chromosomal localization and genomic organization of alpha-amylase genes in rice (Oryza sativa L.). Theor Appl Genet, 1991, 82: 481-488 [15] Yu S M, Kuo Y H, Sheu G, Sheu Y J, Liu L F. Metabolic derepression of alpha-amylase gene expression in suspension- cultured cells of rice. J Biol Chem, 1991, 266: 21131-21137 [16] Itoh K, Yamaguchi J, Huang N, Rodriguez R L, Akazawa T, Shimamoto K. Developmental and hormonal regulation of rice [alpha]-amylase (RAmy1A)-gusA fusion genes in transgenic rice seeds. Plant Physiol, 1995, 107: 25-31 [17] Mitsui T, Yamaguchi J, Akazawa T. Physicochemical and serological characterization of rice [alpha]-amylase isoforms and identification of their corresponding genes. Plant Physiol, 1996, 110: 1395-1404 [18] Chen M H, Liu L F, Chen Y R, Wu H K, Yu S M. Expression of -amylases, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient. Plant J, 1994, 6: 625-636 [19] Tetlow I J, Morell M K, Emes M J. Recent developments in understanding the regulation of starch metabolism in higher plants. J Exp Bot, 2004, 55: 2131-2145 [20] Zeeman S C, Smith S M, Smith A M. The breakdown of starch in leaves. New Phytol, 2004, 163: 247-261 [21] Stanley D, Fitzgerald A M, Farnden K J F, MacRae E A. Characterization of putative α-amylases from apple (Malus domestica) and Arabidopsis thaliana. Biologia, Bratislava, 2002, 57(suppl 11): 137-148 [22] Huang N, Stebbins G L, Rodriguez R L. Classification and evolution of a-amylase genes in plants. Proc Natl Acad Sci USA, 1992, 89: 7526-7530 [23] Sutliff T D, Huang N, Litts J C, Rodriguez R L. Characterization of an a-amylase multigene cluster in rice. Plant Mol Biol, 1991, 16: 579-591 [24] Abe R, Chiba Y, Nakajima T. Characterization of the functional module responsible for the low temperature optimum of a rice a-amylase (Amy3E). Biologia, Bratislava, 2002, 57(suppl 11): 197-202 [25] Karrer E E, Litts J C, Rodriguez R L. Differential expression of a-amylase genes in germinating rice and barley seeds. Plant Mol Biol, 1991, 16: 797-805 [26] Umemura T A, Perata P, Futsuhara Y, Yamaguch J. Sugar sensing and a-amylase gene repression in rice embryos. Planta, 1998, 204: 420-428 [27] Karrer E E, Chandler J M, Foolad M R, Rodriguez R L. Correlation between a-amylase gene expression and seedling vigor in rice. Euphytica, 1993, 66: 163-169 [28] Huang J R, Toyofuku K, Yamaguchi J, Akita S. Expression of a-amylase isoforms and the RAmy1A gene in rice (Oryza sativa L.) during seed germination, and itsrelationship with coleoptile length in submerged soil. Plant Prod Sci, 2000, 3: 32-37 [29] Washio K, Ishikawa K. Structure and expression during the germination of rice seeds of the gene for a carboxypeptidase. Plant Mol Biol, 1992, 19: 631-640 [30] Moritaa A, Umemurab T A, Kuroyanagib M, Futsuharab Y, Perata P, Yamaguchia J. Functional dissection of a sugar-repressed a-amylase gene (RAmy1A) promoter in rice embryos. FEBS Lett, 1998, 423: 81-85 [31] Sugimoto N, Takeda G, Nagato Y, Yamaguchi J. Temporal and spatial expression of the a-amylase gene during seed germination in rice and barley. Plant Cell Physiol, 1998, 39: 323-333 [32] Janecek S. alpha-Amylase family: molecular biology and evolution. Prog Biophys Mol Biol, 1997, 67: 67-97 [33] Sánchez D, Ganfornina M D, Gutiérrez G, Marín A. Exon-intron structure and evolution of the lipocalin gene family. Mol Biol Evol, 2003, 20: 775-783 [34] Li W, Liu B, Yu L, Feng D, Wang H, Wang J. Phylogenetic analysis, structural evolution and functional divergence of the 12-oxo-phytodienoate acid reductase gene family in plants. BMC Evol Biol, 2009, 9: 90 [35] Janecek S. Sequence similarities and evolutionary relationships of microbial, plant and animal a-amylases. Eur J Biochem, 1994, 224: 519-524 Doolittle W F. The Origin and function of intervening sequences in DNA: A review. Am Nat, 1987, 130: 915-928 |
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