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Gene Review

BES1  -  protein brassinazole-resistant 2

Arabidopsis thaliana

Synonyms: 107 PROTEIN, BRASSINAZOLE-RESISTANT 2, BRI1-EMS-SUPPRESSOR 1, BZR2, F18O14.7, ...
 
 
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High impact information on BES1

  • BES1 interacts with a basic helix-loop-helix protein, BIM1, to synergistically bind to E box (CANNTG) sequences present in many BR-induced promoters [1].
  • We showed previously that a novel protein, BES1, accumulates in the nucleus in response to BRs, where it plays a role in BR-regulated gene expression; however, the mechanism by which BES1 regulates gene expression is unknown [1].
  • BES1 is phosphorylated and appears to be destabilized by the glycogen synthase kinase-3 (GSK-3) BIN2, a negative regulator of the BR pathway [2].
  • We identified bes1, a semidominant suppressor of bri1, which exhibits constitutive BR response phenotypes including long and bending petioles, curly leaves, accelerated senescence, and constitutive expression of BR-response genes [2].
  • Microarray technology has been used extensively to provide a global view of BR genomic effects, as well as a specific set of target genes for BES1 and BZR1 [3].
 

Biological context of BES1

  • BES1 accumulates in the nucleus in response to brassinosteroids to regulate gene expression and promote stem elongation [2].
  • Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL [4].
  • Analysis of the complete Arabidopsis genome sequence revealed 107 genes encoding MADS-box proteins, of which 84% are of unknown function [5].
 

Associations of BES1 with chemical compounds

  • Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1 [4].
  • Homologous genes isolated from maize (Zea mays; mis1), barley (Hordeum vulgare; bis1), wheat (Triticum aestivum; wis1), and Arabidopsis encode proteins that are highly similar (76%-82%) to the FIS1 protein [6].
 

Other interactions of BES1

  • Confocal microscopic analysis indicated that both BES1 and BZR1 proteins were mainly localized in the nucleus [7].

References

  1. A new class of transcription factors mediates brassinosteroid-regulated gene expression in Arabidopsis. Yin, Y., Vafeados, D., Tao, Y., Yoshida, S., Asami, T., Chory, J. Cell (2005) [Pubmed]
  2. BES1 accumulates in the nucleus in response to brassinosteroids to regulate gene expression and promote stem elongation. Yin, Y., Wang, Z.Y., Mora-Garcia, S., Li, J., Yoshida, S., Asami, T., Chory, J. Cell (2002) [Pubmed]
  3. Molecular mechanisms of steroid hormone signaling in plants. Vert, G., Nemhauser, J.L., Geldner, N., Hong, F., Chory, J. Annu. Rev. Cell Dev. Biol. (2005) [Pubmed]
  4. Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis. Mora-García, S., Vert, G., Yin, Y., Caño-Delgado, A., Cheong, H., Chory, J. Genes Dev. (2004) [Pubmed]
  5. Molecular and phylogenetic analyses of the complete MADS-box transcription factor family in Arabidopsis: new openings to the MADS world. Parenicová, L., de Folter, S., Kieffer, M., Horner, D.S., Favalli, C., Busscher, J., Cook, H.E., Ingram, R.M., Kater, M.M., Davies, B., Angenent, G.C., Colombo, L. Plant Cell (2003) [Pubmed]
  6. A plant gene up-regulated at rust infection sites. Ayliffe, M.A., Roberts, J.K., Mitchell, H.J., Zhang, R., Lawrence, G.J., Ellis, J.G., Pryor, T.J. Plant Physiol. (2002) [Pubmed]
  7. Two putative BIN2 substrates are nuclear components of brassinosteroid signaling. Zhao, J., Peng, P., Schmitz, R.J., Decker, A.D., Tax, F.E., Li, J. Plant Physiol. (2002) [Pubmed]
 
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