Yeast transcription factor

Figure 9.12 Schematic diagram of the structure of the heterodimeric yeast transcription factor Mat a2-Mat al bound to DNA. Both Mat o2 and Mat al are homeodomains containing the helix-turn-helix motif. The first helix in this motif is colored blue and the second, the recognition helix, is red. (a) The assumed structure of the Mat al homeodomain in the absence of DNA, based on Its sequence similarity to other homeodomains of known structure, (b) The structure of the Mat o2 homeodomain. The C-terminal tail (dotted) is flexible in the monomer and has no defined structure, (c) The structure of the Mat a 1-Mat a2-DNA complex. The C-terminal domain of Mat a2 (yellow) folds into an a helix (4) in the complex and interacts with the first two helices of Mat a2, to form a heterodimer that binds to DNA. (Adapted from B.J. Andrews and M.S. Donoviel, Science 270 251-253, 1995.)...

Yeast transcription factor GAL4 contains a binuclear zinc cluster in its DNA-binding domain... 

The leucine zipper motif (see Chapter 3) was first recognized in the amino acid sequences of a yeast transcription factor GCN4, the mammalian transcription factor C/EBP, and three oncogene products, Fos, Jun and Myc, which also act as transcription factors. When the sequences of these proteins are plotted on a helical wheel, a remarkable pattern of leucine residues... 

Figure 2.21 Zinc-finger protein from the yeast transcription factors SWI as visualized using Wavefunction, Inc. Spartan 02 for Windows from PDB data deposited as 1NCS. See text for visualization details. Printed with permission of Wavefunction, Inc., Irvine, CA. (See color plate.)...

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 ...

Gabrielsen, O. S., Homes, E., Komes, L., Ruet, A., and Oyen, T. B. (1989) Magnetic DNA affinity purification of yeast transcription factor T—a new purification principle for the ultrarapid isolation of near homogenous factor. Nucleic Acids Res. 17,6253-6267. 

Fig. 3. The structure of the 33-residue region of yeast transcription factor GCN4 is a two-stranded coiled coil, and is viewed here perpendicular to its long axis. The chains each have a heptad substructure and an a-helical conformation. Because GCN4 contains leucine residues in each d position, except for the most C-terminal one, the structure is commonly referred to as a leucine zipper (PDB coordinate reference number 2ZTA). The pitch length of the left-handed coiled coil has an average value of about 20.4 nm (Harbury et al, 1993 Kuhnel et al, 2004).

Chan, C.K., Htibner, S., Hu, W. and Jans, D A. (1998) Mutual exclusivity of DNA binding and nuclear localization signal recognition by the yeast transcription factor GAL4 implications for nonviral DNA delivery. Gene Then, 5, 1204-1212. 

The various aspects of our approach are demonstrated below within the context of a two-stranded coiled-coil polypeptide model that was designed to mimic the disulfide cross-linked two-stranded coiled-coil from the yeast transcription factor GCN4 [68-74] which was used by Hochstrasser and coworkers in their pioneering SM-FRET experiment. [30,33]... 

It is also of interest to compare our results with experiment. The experimental study most closely related to the model considered here is the SM-FRET assay by Hochstrasser and co-workers on the disulfide cross-linked two-stranded coiled-coil from the yeast transcription factor GCN4. [30,33] Our results appear to be consistent with many of the experimental observations reported in Refs. [30,33], For example, surface-immobilization in the folded state has a rather small effect on the R distribution, the folded and unfolded states are seen to correspond to narrow and broad R distributions, respectively, and conformational dynamics is seen to be characterized by a wide dynamical range in the midpoint and unfolded states. Our analysis can also help in the interpretation of the experimental results. For example, surface-... 

J. J. Kang, D. T. Auble, J. A. Ranish, and S. Hahn. Analysis of the yeast transcription factor TFIIA distinct functional regions and a polymerase n-spectfic role in basal and activated transcription. Mol Cell Bid, IS (3), 1234-1243, 1995. 

Figure 31.19. Gal4 Binding Sites. The yeast transcription factor GAL4 binds to DNA sequences of the form 5 -CGG(N) 1 lCCG-3. Two zinc-based domains are present in the DNA-binding region of this protein. These domains contact the 5 -CGG-3 sequences, leaving the center of the site uncontacted.

Delahodde. A.. Delaveau. T, and Jacq, C. (1995) Positive autoregulation of the yeast transcription factor Pdr3p, which is involved in control of drug resistance. Molecular and CeUular Biology, 15. 4043-4051. 

Gregori, C., Schuller, C., Frohner, I.E., Ammerer, G., and Kuchler, K. (2008) Weak organic acids trigger conformational changes of the yeast transcription factor Warl in vivo to elicit stress adaptation. The Journal of Biological Chemistry, 283 (37), 25752-25764. 

Kuge, S., Toda, T., lizuka, N and Nomoto, A. (1998) Crml (Xpol) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress. Genes to CeUs, 3, 521-532. 

Kndo, N., Taoka, H., Toda, T., Yoshida, M., Horinonchi, S. (1999). A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Papl. 

Covalent modification by methylation or acetylation at Arg or Lys residues can be used to regulate the interaction of transcription factors with other regulatory proteins. As an example, Arg methylation of the transcription factor Statl regulates its dephosphorylation by protein tyrosine phosphatases (Zhu et al., 2002). Acetylation of Lys residues controls the activity of the yeast transcription factor GATA-1 (Boyes et al., 1998). 

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