The light-saturated rate of photosynthetic O 2 evolution in Chlamydomonas reinhardtii declined by approximately 75% on a per-cell basis after 4 d of P starvation or 1 d of S starvation. Quantitation of the partial reactions of photosynthetic electron transport demonstrated that the light-saturated rate of photosystem (PS) I activity was unaffected by P or S limitation, whereas lightsaturated PSII activity was reduced by more than 50%. This decline in PSII activity correlated with a decline in both the maximal quantum efficiency of PSII and the accumulation of the secondary quinone electron acceptor of PSII nonreducing centers (PSII centers capable of performing a charge separation but unable to reduce the plastoquinone pool). In addition to a decline in the light-saturated rate of O 2 evolution, there was reduced efficiency of excitation energy transfer to the reaction centers of PSII (because of dissipation of absorbed light energy as heat and because of a transition to state 2). These findings establish a common suite of alterations in photosynthetic electron transport that results in decreased linear electron flow when C. reinhardtii is limited for either P or S. It was interesting that the decline in the maximum quantum efficiency of PSII and the accumulation of the secondary quinone electron acceptor of PSII nonreducing centers were regulated specifically during S-limited growth by the SacI gene product, which was previously shown to be critical for the acclimation of C. reinhardtii to S limitation

Understanding the ways in which phosphorus metabolism is regulated in photosynthetic eukaryotes is critical for optimizing crop productivity and managing aquatic ecosystems in which phosphorus can be a major source of pollution. Here we describe a gene encoding a regulator of phosphorus metabolism, designated Psr1 (phosphorus starvation response), from a photosynthetic eukaryote. The Psr1 protein is critical for acclimation of the unicellular green alga Chlamydomonas reinhardtii to phosphorus starvation. The N-terminal half of Psr1 contains a region similar to myb DNA-binding domains and the C-terminal half possesses glutamine-rich sequences characteristic of transcriptional activators. The level of Psr1 increases at least 10-fold upon phosphate starvation, and immunocytochemical studies demonstrate that this protein is nuclear-localized under both nutrientreplete and phosphorus-starvation conditions. Finally, Psr1 and angiosperm proteins have domains that are similar, suggesting a possible role for Psr1 homologs in the control of phosphorus metabolism in vascular plants. With the identification of regulators such as Psr1 it may become possible to engineer photosynthetic organisms for more efficient utilization of phosphorus and to establish better practices for the management of agricultural lands and natural ecosystems. P hosphorus (P) is a major component of nucleic acids and phospholipids and is present in the biosphere as the oxidized anion, phosphate (P i ). P i is not easily accessible to most plants and microbes because it forms insoluble precipitates with common cations or is covalently bound to organic molecules (1-3). Crop yields are limited by P availability, and, consequently, P, in the form of P i , is an important component of commercial fertilizers. A considerable proportion of this ''supplementary'' P i is leached from agricultural fields and deposited into aquatic ecosystems, triggering rapid algal proliferation (algal blooms), which leads to eutrophication and fish kills (2). The sustainability of agricultural yields and quality of aquatic ecosystems would benefit from more efficient acquisition and utilization of P. Efficient P utilization by crop plants would decrease our dependence on rock P i reserves, the mining of which has serious economic and ecological consequences (3). Thus, a more complete understanding of P utilization in plants has significant implications with respect to both the environment and world agriculture.P limitation triggers a suite of ''starvation responses'' in most organisms. These responses can be divided into two categories, the P-specific responses and the general responses (4-6). The P-specific responses promote efficient mobilization and acquisition of P from extracellular and intracellular stores (e.g., synthesis and secretion of phosphatases with broad substrate specificity, accumulation of high affinity P i transporters) (5, 7). The general responses allow for long-term survival by coordinating the metabolism of the cell to nutrient availability and growth po...