Nature 334, 631 - 633 (18 August 1988); doi:10.1038/334631a0

Yeast activators stimulate plant gene expression

Jun Ma^*, Elisabeth Przibilla^†, Jim Hu^†, Lawrence Bogorad^† & Mark Ptashne^*

^*Department of Biochemistry and Molecular Biology and
^†Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138, USA

GAL4 is a transcriptional activator found in yeast^1,2. Two distinct functions of the protein are required for its activity³⁻⁵: one directs sequen1ce-specific DNA binding, and another interacts with some other component of the transcriptional machinery, for example, RNA polymerase II or a TATA-binding protein. Two short regions of GAL4 function as 'activating sequences' when attached to the DNA-binding portion of GAL4 (ref. 6) and these regions can be replaced by a large number of peptides encoded by Escherichia coli genomic DNA fragments⁷ or by a synthetic peptide designed to form an amphiphilic -helix⁸. All of these activating sequences, like that found in another yeast activator, GCN4 (refs 9, 10) bear an excess negative charge (also see ref. 11). GAL4 and its derivatives that are active in yeast stimulate transcription in mammalian cells when GAL4 binding sites are introduced upstream of a mammalian gene^12,13; similarly, GAL4 activates transcription in Drosophila cells¹⁴. Here we show that GAL4 derivatives stimulate gene expression in plant cells.

References

1.	Oshima, Y. in Molecular Biology of the Yeast Saccharomyces cerevisiae: Metabolism and Gene Expression (eds. Strathern, J. N., Jones, E. W. & Broach, J. R.) 159−180 (Cold Spring Harbor Laboratory, New York, 1982). | ChemPort |
2.	Johnston, M. Microbiol. Rev. 51, 458−476 (1987). | PubMed | ISI | ChemPort |
3.	Brent, R. & Ptashne, M. Cell 43 729−736 (1985). | Article | PubMed | ISI | ChemPort |
4.	Keegan, L., Gill, G. & Ptashne, M. Science 231, 699−704 (1986). | PubMed | ISI | ChemPort |
5.	Ptashne, M. Nature 322, 697−701 (1986). | Article | PubMed | ChemPort |
6.	Ma, J. & Ptashne, M. Cell 48, 847−853 (1987). | Article | PubMed | ISI | ChemPort |
7.	Ma, J. & Ptashne, M. Cell 51, 113−119 (1987). | Article | PubMed | ISI | ChemPort |
8.	Giniger, E. & Ptashne, M. Nature 330, 670−672 (1987). | Article | PubMed | ISI | ChemPort |
9.	Hope, I. & Struhl, K. Cell 46, 885−894 (1986). | Article | PubMed | ISI | ChemPort |
10.	Struhl, K. Cell 49, 294−297 (1987).
11.	Gill, G. & Ptashne, M. Cell 51, 121−126 (1987). | Article | PubMed | ChemPort |
12.	Kakidani, H. & Ptashne, M. Cell 52, 161−167 (1988). | Article | PubMed | ISI | ChemPort |
13.	Webster, N., Jin, J. R., Green, S., Hollis, M. & Chambon, P. Cell 52, 169−178 (1988). | Article | PubMed | ISI | ChemPort |
14.	Fisher, J., Giniger, E., Maniatis, T. & Ptashne, M. Nature 332, 853−856 (1988). | Article | PubMed | ISI | ChemPort |
15.	Bevan, M., Barnes, W. M. & Chilton, M. D. Nucleic Acids Res. 11, 369−385 (1983). | PubMed | ISI | ChemPort |
16.	Alton, N. K. & Vapnek, D. Nature 282, 864−869 (1979). | PubMed | ISI | ChemPort |
17.	Odell, J. T., Nagy, F. & Chua, N.-H. Nature 313, 810−812 (1985). | Article | PubMed | ISI | ChemPort |
18.	Giniger, E., Varnum, S. & Ptashne, M. Cell 40, 767−774 (1985). | Article | PubMed | ISI | ChemPort |
19.	Jefferson, R. A., Burgess, S. M. & Hirsch, D. Proc. natn. Acad. Sci. U.S.A. 83, 8447−8451 (1986). | ChemPort |
20.	Jefferson, R. A. Pl. molec. Biol. Reporter 5, 387−405 (1987). | ChemPort |
21.	Nagy, J. I. & Maliga, P. Z. Pflanzenphysiol. 78, 435−455 (1976).
22.	Fromm, M., Taylor, L. P. & Walbot, V. Proc. natn. Acad. Sci. U.S.A. 82, 5824−5828 (1985). | ChemPort |