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Gene Review

LOC548210  -  alpha-amylase 1

Hordeum vulgare

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Disease relevance of LOC548210


High impact information on LOC548210

  • Using the double-stranded RNA interference technique, we show that HvABI5 and HvVP1 are necessary for the ABA induction of gene expression but have no effect on another hormone-regulated process, the gibberellin-induced and ABA-suppressed expression of alpha-amylase [6].
  • Three novel MYB proteins with one DNA binding repeat mediate sugar and hormone regulation of alpha-amylase gene expression [7].
  • Although the ABA-induced Ser/Thr protein kinase, PKABA1, is known to suppress GA-induced alpha-amylase expression, PKABA1 RNAi did not hamper the inhibitory effect of ABA on the expression of alpha-amylase, indicating that a PKABA1-independent signaling pathway also may exist [8].
  • Transient expression assays also showed that these three OsMYBSs cooperate with a GA-regulated transcription factor, HvMYBGa, in the transactivation of a low-pI barley alpha-amylase gene promoter in the absence of GA [7].
  • All alpha-amylase genes isolated from cereals contain a TATCCA element or its variants at positions approximately 90 to 150 bp upstream of the transcription start sites [7].

Chemical compound and disease context of LOC548210


Biological context of LOC548210

  • Our results indicate that the GAMyb is the sole GA-regulated transcription factor required for transcriptional activation of the high-pI alpha-amylase promoter [10].
  • We demonstrated in transient expression experiments that GAMyb activates transcription of a high-pI alpha-amylase promoter fused to a beta-glucuronidase reporter gene in the absence of GA [10].
  • We propose that the TAACAAA box is a gibberellin response element, that the TATCCAC box acts cooperatively with the TAACAAA box to give a high level of GA-regulated expression, and that together these motifs form important components of a gibberellin response complex in high-pI alpha-amylase genes [11].
  • The promoters of a majority of cereal alpha-amylase genes contain three highly conserved sequences (gibberellin response element, box I, and pyrimidine box) [12].
  • Using a barley aleurone transient expression system, we have now localized the site of action of PKABA1 relative to other signal transduction components governing the expression of alpha-amylase [13].

Anatomical context of LOC548210


Associations of LOC548210 with chemical compounds


Enzymatic interactions of LOC548210

  • Activities of alpha-amylase and alpha-glucosidase were positively and significantly correlated with the seed extracts' abilities to hydrolyze all three starches. beta-Amylase was only significantly correlated with hydrolysis of boiled soluble starch [20].

Other interactions of LOC548210


Analytical, diagnostic and therapeutic context of LOC548210


  1. Characterization of wheat germ protein synthesis initiation factor eIF-4C and comparison of eIF-4C from wheat germ and rabbit reticulocytes. Timmer, R.T., Lax, S.R., Hughes, D.L., Merrick, W.C., Ravel, J.M., Browning, K.S. J. Biol. Chem. (1993) [Pubmed]
  2. Abscisic acid stimulation of phospholipase D in the barley aleurone is G-protein-mediated and localized to the plasma membrane. Ritchie, S., Gilroy, S. Plant Physiol. (2000) [Pubmed]
  3. Rye flour allergens associated with baker's asthma. Correlation between in vivo and in vitro activities and comparison with their wheat and barley homologues. García-Casado, G., Armentia, A., Sánchez-Monge, R., Malpica, J.M., Salcedo, G. Clin. Exp. Allergy (1996) [Pubmed]
  4. Barley aleurone layer cell protoplasts as a transient expression system. Gopalakrishnan, B., Sonthayanon, B., Rahmatullah, R., Muthukrishnan, S. Plant Mol. Biol. (1991) [Pubmed]
  5. An E. coli expression system for the extracellular secretion of barley alpha-amylase. Lee, C.C., Wong, D.W., Robertson, G.H. J. Protein Chem. (2001) [Pubmed]
  6. The transcription factors HvABI5 and HvVP1 are required for the abscisic acid induction of gene expression in barley aleurone cells. Casaretto, J., Ho, T.H. Plant Cell (2003) [Pubmed]
  7. Three novel MYB proteins with one DNA binding repeat mediate sugar and hormone regulation of alpha-amylase gene expression. Lu, C.A., Ho, T.H., Ho, S.L., Yu, S.M. Plant Cell (2002) [Pubmed]
  8. Molecular dissection of the gibberellin/abscisic acid signaling pathways by transiently expressed RNA interference in barley aleurone cells. Zentella, R., Yamauchi, D., Ho, T.H. Plant Cell (2002) [Pubmed]
  9. Isolation, characterization and inhibition by acarbose of the alpha-amylase from Lactobacillus fermentum: comparison with Lb. manihotivorans and Lb. plantarum amylases. Talamond, P., Desseaux, V., Moreau, Y., Santimone, M., Marchis-Mouren, G. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2002) [Pubmed]
  10. Gibberellin-regulated expression of a myb gene in barley aleurone cells: evidence for Myb transactivation of a high-pI alpha-amylase gene promoter. Gubler, F., Kalla, R., Roberts, J.K., Jacobsen, J.V. Plant Cell (1995) [Pubmed]
  11. Gibberellin-responsive elements in the promoter of a barley high-pI alpha-amylase gene. Gubler, F., Jacobsen, J.V. Plant Cell (1992) [Pubmed]
  12. Gibberellin treatment stimulates nuclear factor binding to the gibberellin response complex in a barley alpha-amylase promoter. Sutliff, T.D., Lanahan, M.B., Ho, T.H. Plant Cell (1993) [Pubmed]
  13. Gibberellin/abscisic acid antagonism in barley aleurone cells: site of action of the protein kinase PKABA1 in relation to gibberellin signaling molecules. Gómez-Cadenas, A., Zentella, R., Walker-Simmons, M.K., Ho, T.H. Plant Cell (2001) [Pubmed]
  14. C-terminal processing of barley alpha-amylase 1 in malt, aleurone protoplasts, and yeast. Søgaard, M., Olsen, F.L., Svensson, B. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  15. Heat shock causes destabilization of specific mRNAs and destruction of endoplasmic reticulum in barley aleurone cells. Belanger, F.C., Brodl, M.R., Ho, T.H. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  16. Redox-sensitive target detection in gibberellic acid-induced barley aleurone layer. Maya-Ampudia, V., Bernal-Lugo, I. Free Radic. Biol. Med. (2006) [Pubmed]
  17. A role for arabinogalactan proteins in gibberellin-induced alpha-amylase production in barley aleurone cells. Suzuki, Y., Kitagawa, M., Knox, J.P., Yamaguchi, I. Plant J. (2002) [Pubmed]
  18. Primer extension studies on alpha-amylase mRNAs in barley aleurone. I. Characterization and quantification of the transcripts. Chandler, P.M., Huiet, L. Plant Mol. Biol. (1991) [Pubmed]
  19. 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. Søgaard, M., Kadziola, A., Haser, R., Svensson, B. J. Biol. Chem. (1993) [Pubmed]
  20. A quantitative assessment of the importance of barley seed alpha-amylase, beta-amylase, debranching enzyme, and alpha-glucosidase in starch degradation. Sun, Z.T., Henson, C.A. Arch. Biochem. Biophys. (1991) [Pubmed]
  21. The role of cereal and fungal amylases in cereal flour hypersensitivity. Sandiford, C.P., Tee, R.D., Taylor, A.J. Clin. Exp. Allergy (1994) [Pubmed]
  22. Mutational analysis of target enzyme recognition of the beta-trefoil fold barley alpha-amylase/subtilisin inhibitor. Bønsager, B.C., Nielsen, P.K., Abou Hachem, M., Fukuda, K., Praetorius-Ibba, M., Svensson, B. J. Biol. Chem. (2005) [Pubmed]
  23. Barley alpha-amylase genes. Quantitative comparison of steady-state mRNA levels from individual members of the two different families expressed in aleurone cells. Khursheed, B., Rogers, J.C. J. Biol. Chem. (1988) [Pubmed]
  24. Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2. Svensson, B., Gibson, R.M., Haser, R., Astier, J.P. J. Biol. Chem. (1987) [Pubmed]
  25. Isolation and sequence analysis of a barley alpha-amylase cDNA clone. Rogers, J.C., Milliman, C. J. Biol. Chem. (1983) [Pubmed]
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