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Plant Physiol, February 2002, Vol. 128, pp. 463-471

Oxygen Deficiency Responsive Gene Expression in Chlamydomonas reinhardtii through a Copper-Sensing Signal Transduction Pathway1

Jeanette M. Quinn, Mats Eriksson,2 Jeffrey L. Moseley, and Sabeeha Merchant*

Department of Chemistry and Biochemistry (J.M.Q., M.E., J.L.M., S.M.) and Molecular Biology Institute (J.M., S.M.), University of California, Los Angeles, California 90095-1569

Chlamydomonas reinhardtii activates Cpx1, Cyc6, and Crd1, encoding, respectively, coproporphyrinogen oxidase, cytochrome c6, and a novel di-iron enzyme when transferred to oxygen-deficient growth conditions. This response is physiologically relevant because C. reinhardtii experiences these growth conditions routinely, and furthermore, one of the target genes, Crd1, is functionally required for normal growth under oxygen-depleted conditions. The same genes are activated also in response to copper-deficiency through copper-response elements that function as target sites for a transcriptional activator. The core of the copper-response element, GTAC, is required also for the hypoxic response, as is a trans-acting locus, CRR1. Mercuric ions, which antagonize the copper-deficiency response, also antagonize the oxygen-deficiency response of these target genes. Taken together, these observations suggest that the oxygen- and copper-deficiency responses share signal transduction components. Nevertheless, whereas the copper-response element is sufficient for the nutritional copper response, the oxygen-deficiency response requires, in addition, a second cis-element, indicating that the response to oxygen depletion is not identical to the nutritional copper response. The distinction between the two responses is also supported by comparative analysis of the response of the target genes, Cyc6, Cpx1, and Crd1, to copper versus oxygen deficiency. A Crr1-independent pathway for Hyd1 expression in oxygen-depleted C. reinhardtii demonstrates the existence of multiple oxygen/redox-responsive circuits in this model organism.


1 This work was supported by the National Institutes of Health (grant no. GM42143). M.E. was supported, in part, by a European Molecular Biology Organization Long-Term Fellowship, and J.L.M., was supported, in part, by the Molecular Biology Ph.D. program and a Dissertation Year Fellowship from the Graduate Division of the University of California (Los Angeles).

2 Present address: Department of Plant Physiology, Umeå University, S-901 87 Umeå, Sweden.

* Corresponding author; e-mail merchant{at}chem.ucla.edu; fax 310-206-1035.

© 2002 American Society of Plant Physiologists



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