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JXB Advance Access originally published online on October 22, 2004
Journal of Experimental Botany 2005 56(409):145-153; doi:10.1093/jxb/eri008
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Journal of Experimental Botany, Vol. 56, No. 409, © Society for Experimental Biology 2005; all rights reserved

RESEARCH PAPER

Phosphate deficiency regulates phosphoenolpyruvate carboxylase expression in proteoid root clusters of white lupin

Enrique Peñaloza1,*, Gastón Muñoz1, Haroldo Salvo-Garrido1, Herman Silva2 and Luis J. Corcuera3

1Instituto de Investigaciones Agropecuarias, Unidad de Biotecnología, INIA Carillanca, Casilla 58-D, Temuco, Chile
2Laboratorio de Genética Molecular Vegetal, Millenium Nucleus in Plant Cell Biology P02-009-F, Departamento de Biología, Universidad de Chile, 7800024 Nuñoa, Santiago, Chile
3Departamento de Botánica, Universidad de Concepción, Casilla 160-C, Concepción, Chile

* To whom correspondence should be addressed. Fax: +56 45 216112. E-mail: epenaloz{at}carillanca.inia.cl

Proteoid roots play a major role in enabling white lupin (Lupinus albus L.) to adapt to phosphate (Pi) deficiency. Such roots release citrate from proteoid rootlets, which allows this species to mobilize Pi from sparingly soluble Pi sources. Release of citrate is preceded by a significant accumulation of organic acids, in which a Pi deficiency-inducible phosphoenolpyruvate carboxylase (PEPC) activity has been involved. To gain an insight into this adaptive mechanism, the expression of three different transcripts coding for PEPC was examined in proteoid rootlets of Pi-starved and Pi-starved-and-rescued white lupin. Semi-quantitative reverse transcriptase (RT)-PCR experiments performed with gene-specific primers targeted to the 3'-end region of the corresponding cDNAs revealed that the transcripts for these three PEPCs differentially accumulate in both Pi-starved and Pi-starved-and-rescued proteoid rootlets. Semi-quantitative RT-PCR analysis in Pi-starved proteoid rootlets sampled at different times after being rescued from Pi deficiency showed that Pi levels differentially down-regulated the three PEPC transcripts. RT-PCR experiments were further extended to Pi-starved and Pi-fed whole roots, cotyledons, and leaves on which a tissue-specific, Pi-dependent PEPC expression was observed. These results indicate that there exists at least three different transcripts coding for PEPC in proteoid root clusters of white lupin, whose expression are differentially regulated by Pi.

Key words: Lupinus albus, PEPC activity, PEPC expression, proteoid rootlets


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K. Zhou, M. Yamagishi, M. Osaki, and K. Masuda
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J. Exp. Bot., July 1, 2008; 59(10): 2749 - 2756.
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