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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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