You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Gibberellin/Abscisic Acid Antagonism in Barley Aleurone Cells: Site of Action of the Protein Kinase PKABA1 in Relation to Gibberellin Signaling Molecules
Aurelio Gómez-Cadenas, Rodolfo Zentella, Mary Kay Walker-Simmons and Tuan-Hua David Ho
The Plant Cell
Vol. 13, No. 3 (Mar., 2001), pp. 667-679
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/3871414
Page Count: 13
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
The antagonism between gibberellins (GA) and abscisic acid (ABA) is an important factor regulating the developmental transition from embryogenesis to seed germination. In barley aleurone layers, the expression of genes encoding α-amylases and proteases is induced by GA but suppressed by ABA. It has been shown that an ABA-induced protein kinase, PKABA1, mediates the ABA suppression of α-amylase expression. 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 α-amylase. The expression of α-amylase can be transactivated by the transcription factor GAMyb, which is itself induced by GA. A truncated GAMyb containing the DNA binding domain but lacking the transactivation domain prevents the GA induction of α-amylase, further supporting the notion that GAMyb mediates the GA induction of α-amylase expression. Although ABA and PKABA1 strongly inhibit the GA induction of α-amylase, they have no effect on GAMyb-transactivated α-amylase expression. Using a GAMyb promoter-β-glucuronidase construct, we also show that both ABA and PKABA1 repress the GA induction of GAMyb. In the slender mutant, GAMyb and α-amylase are highly expressed, even in the absence of GA. However, this constitutive expression can still be inhibited by ABA, PKABA1, or an inhibitor of cGMP synthesis. On the basis of these observations, we suggest that PKABA1 acts upstream from the formation of functional GAMyb but downstream from the site of action of the Slender gene product. Because PKABA1 inhibits the GA induction of the GAMyb promoter-β-glucuronidase construct, it appears that at least part of the action of PKABA1 is to downregulate GAMyb at the transcriptional level.
The Plant Cell © 2001 American Society of Plant Biologists (ASPB)