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BZIP transcription factor

Jakoby, M. et al., bZIP transcription factors in Arahidopsis. Trends Plant Set, 1, 106, 2002. [Pg.213]

Figure 4.30 Proposed mechanisms for bZIP transcription factor function. Stable association of the bZIP dimer with DNA can occur via a monomer or dimer pathway. Binding of both monomer and dimer is diffusion limited. Analysis of the kinetics of both pathways suggests that the monomer pathway may have an overall kinetic advantage. Figure 4.30 <a href="/info/fi_proposed_mechanism">Proposed mechanisms</a> for bZIP transcription factor function. Stable association of the bZIP dimer with DNA can occur via a monomer or dimer pathway. Binding of both monomer and dimer is <a href="/info/diffusion_limitation">diffusion limited</a>. Analysis of the kinetics of both pathways suggests that the monomer pathway may have an <a href="/info/overall_kinetics">overall kinetic</a> advantage.
Alarco, A.M. and Raymond, M. (1999) The bZip transcription factor Caplp is involved in multidrug resistance and oxidative stress response in Candida albicans. Journal of Bacteriology, 181, 700-708. [Pg.188]

Glover JN, Harrison SC (1995) Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373 257-261 [Pg.78]

J. N. Glover and S. C. Harrison. Crystal structure of the heterodimenc bZIP transcription factor c-Fbs-c-Jun bound to DNA. Nature, 373, 257—261, 1995- [Pg.186]

Husberg C, Murphy P, Martin E, Kolsto AB. 2001. Two domains of the human bZIP transcription factor TCF11 are nec- [Pg.258]

Berger, C., et al.. Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor. FEBS letters, 1998, 425, 14-18. [Pg.111]

Wellmer, F., Schafer, E., and Harter, K., The DNA binding properties of the parsley bZIP transcription factor CPRF4a are regulated by light. J. Biol Chem., 276, 6274, 2001. [Pg.213]

Figure 5-36 Stereoscopic diagrams showing some of the interactions between an N-terminal helical domain of the yeast transcription factor GCN4-bZIP, a leucine zipper protein, and a specific palindromic DNA binding site Figure 5-36 Stereoscopic diagrams showing some of the <a href="/info/a_interactions_between_co_and">interactions between</a> an N-terminal helical domain of the <a href="/info/yeast_transcription_factor">yeast transcription factor</a> GCN4-bZIP, a <a href="/info/leucine_zipper_protein">leucine zipper protein</a>, and a specific palindromic DNA binding site
George H, Terracol R 1997 The vrille gene of Drosophila is a maternal enhancer of decapentaplegic and encodes a new member of the bZIP family of transcription factors. Genetics 146  [Pg.149]

DNA binding domains called basic domains (rich in basic amino acids), occur in transcription factors in combination with leucine zipper or helix-loop-helix (HLH) dimerization domains (see below). The combination of basic domain and dimerization domain gives these proteins their names of basic leucine zipper proteins (bZIP) or basic HLH proteins, respectively. In each case the dimerization means that two basic domains (one from each monomer) interact with the target DNA. [Pg.192]

In view of the participation of protein kinases and phosphatases in ABA signalling it is likely that constitutively bound transcription factors on ABA inducible genes could be regulated by phosphorylation or dephosphorylation. Activation of transcription by the mammalian bZIP transcription factor CREB is induced by phosphorylation of a serine [Pg.509]


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See also in sourсe #XX -- [ Pg.519 ]




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