First published online April 7, 2006; 10.1105/tpc.105.034041
The Plant Cell 18:1274-1291 (2006)
© 2006 American Society of Plant Biologists
PH4 of Petunia Is an R2R3 MYB Protein That Activates Vacuolar Acidification through Interactions with Basic-Helix-Loop-Helix Transcription Factors of the Anthocyanin Pathway[W]
Francesca Quattrocchio1,
Walter Verweij1,
Arthur Kroon,
Cornelis Spelt,
Joseph Mol and
Ronald Koes2
Institute for Molecular and Cellular Biology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands
2 To whom correspondence should be addressed. E-mail ronald.koes{at}falw.vu.nl; fax 31-20-5987155.
The Petunia hybrida genes ANTHOCYANIN1 (AN1) and AN2 encode transcription factors with a basic-helix-loop-helix (BHLH) and a MYB domain, respectively, that are required for anthocyanin synthesis and acidification of the vacuole in petal cells. Mutation of PH4 results in a bluer flower color, increased pH of petal extracts, and, in certain genetic backgrounds, the disappearance of anthocyanins and fading of the flower color. PH4 encodes a MYB domain protein that is expressed in the petal epidermis and that can interact, like AN2, with AN1 and the related BHLH protein JAF13 in yeast two-hybrid assays. Mutation of PH4 has little or no effect on the expression of structural anthocyanin genes but strongly downregulates the expression of CAC16.5, encoding a protease-like protein of unknown biological function. Constitutive expression of PH4 and AN1 in transgenic plants is sufficient to activate CAC16.5 ectopically. Together with the previous finding that AN1 domains required for anthocyanin synthesis and vacuolar acidification can be partially separated, this suggests that AN1 activates different pathways through interactions with distinct MYB proteins.
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