Transcriptional responses of Trichodesmium to natural inverse gradients of Fe and P availability.

The filamentous diazotrophic cyanobacterium Trichodesmium is responsible for a significant fraction of marine di-nitrogen (N2) fixation. Growth and distribution of Trichodesmium and other diazotrophs in the vast oligotrophic subtropical gyres is influenced by iron (Fe) and phosphorus (P) availability, while reciprocally influencing the biogeochemistry of these nutrients. Here we use observations across natural inverse gradients in Fe and P in the North Atlantic subtropical gyre (NASG) to demonstrate how Trichodesmium acclimates in situ to resource availability. Transcriptomic analysis identified progressive upregulation of known iron-stress biomarker genes with decreasing Fe availability, and progressive upregulation of genes involved in the acquisition of diverse P sources with decreasing P availability, while genes involved in N2 fixation were upregulated at the intersection under moderate Fe and P availability. Enhanced N2 fixation within the Fe and P co-stressed transition region was also associated with a distinct, consistent metabolic profile, including the expression of alternative photosynthetic pathways that potentially facilitate ATP generation required for N2 fixation with reduced net oxygen production. The observed response of Trichodesmium to availability of both Fe and P supports suggestions that these biogeochemically significant organisms employ unique molecular, and thus physiological responses as adaptations to specifically exploit the Fe and P co-limited niche they construct.

Low-light-adapted Prochlorococcus species possess specific antennae for each photosystem.

Prochlorococcus, the most abundant genus of photosynthetic organisms, owes its remarkably large depth distribution in the oceans to the occurrence of distinct genotypes adapted to either low- or high-light niches. The pcb genes, encoding the major chlorophyll-binding, light-harvesting antenna proteins in this genus, are present in multiple copies in low-light strains but as a single copy in high-light strains. The basis of this differentiation, however, has remained obscure. Here we show that the moderate low-light-adapted strain Prochlorococcus sp. MIT 9313 has one iron-stress-induced pcb gene encoding an antenna protein serving photosystem I (PSI)--comparable to isiA genes from cyanobacteria--and a constitutively expressed pcb gene encoding a photosystem II (PSII) antenna protein. By comparison, the very low-light-adapted strain SS120 has seven pcb genes encoding constitutive PSI and PSII antennae, plus one PSI iron-regulated pcb gene, whereas the high-light-adapted strain MED4 has only a constitutive PSII antenna. Thus, it seems that the adaptation of Prochlorococcus to low light environments has triggered a multiplication and specialization of Pcb proteins comparable to that found for Cab proteins in plants and green algae.

Oxyphotobacteria. Antenna ring around photosystem I.

The oceanic picoplankton Prochlorococcus - probably the most abundant photosynthetic organism on our planet - can grow at great depths where light intensity is very low. We have found that the chlorophyll-binding proteins in a deep-living strain of this oxyphotobacterium form a ring around a trimer of the photosystem I (PS I) photosynthetic reaction centre, a clever arrangement that maximizes the capture of light energy in such dim conditions.

Three-dimensional model and characterization of the iron stress-induced CP43'-photosystem I supercomplex isolated from the cyanobacterium Synechocystis PCC 6803.

The cyanobacterium Synechocystis PCC 6803 has been subjected to growth under iron-deficient conditions. As a consequence, the isiA gene is expressed, and its product, the chlorophyll a-binding protein CP43', accumulates in the cell. Recently, we have shown for the first time that 18 copies of this photosystem II (PSII)-like chlorophyll a-binding protein forms a ring around the trimeric photosystem I (PSI) reaction center (Bibby, T. S., Nield, J., and Barber, J. (2001) Nature, 412, 743-745). Here we further characterize the biochemical and structural properties of this novel CP43'-PSI supercomplex confirming that it is a functional unit of approximately 1900 kDa where the antenna size of PSI is increased by 70% or more. Using electron microscopy and single particle analysis, we have constructed a preliminary three-dimensional model of the CP43'-PSI supercomplex and used it as a framework to incorporate higher resolution structures of PSI and CP43 recently derived from x-ray crystallography. Not only does this work emphasize the flexibility of cyanobacterial light-harvesting systems in response to the lowering of phycobilisome and PSI levels under iron-deficient conditions, but it also has implications for understanding the organization of the related chlorophyll a/b-binding Pcb proteins of oxychlorobacteria, formerly known as prochlorophytes.

Iron deficiency induces the formation of an antenna ring around trimeric photosystem I in cyanobacteria.

Although iron is the fourth most abundant element in the Earth's crust, its concentration in the aquatic ecosystems-particularly the open oceans-is sufficiently low to limit photosynthetic activity and phytoplankton growth. Cyanobacteria, a major class of phytoplankton, respond to iron deficiency by expressing the 'iron-stress-induced' gene, isiA(ref. 3). The protein encoded by this gene has an amino-acid sequence that shows significant homology with one of the chlorophyll a-binding proteins (CP43) of photosystem II (PSII). The precise function of the CP43-like protein, here called CP43', has not been elucidated, although there have been many suggestions. Here we show that CP43' associates with photosystem I (PSI) to form a complex that consists of a ring of 18 CP43' molecules around a PSI trimer. This significantly increases the size of the light-harvesting system of PSI. The utilization of a PSII-like protein as an extra antenna for PSI emphasises the flexibility of cyanobacterial light-harvesting systems, and seems to be a strategy which compensates for the lowering of phycobilisome and PSI levels in response to iron deficiency.

Identification of the upper exciton component of the B850 bacteriochlorophylls of the LH2 antenna complex, using a B800-free mutant of Rhodobacter sphaeroides.

In this paper, we report the circular dichroism (CD) spectra of two types of LH2-only mutants of Rhodobacter sphaeroides. In the first, only the wild type LH2 is present, while i the second, the B800 binding site of LH2 has been either destabilized or removed. For the first time, we have identified a band in the CD spectrum of LH2, located at approximately 780 nm, that can be ascribed to the high exciton component of the B850 band. The experimental spectra have been modeled by theoretical calculations. On this basis, the average interaction strength between the monomers in the B850 ring can be estimated to be approximately 300 cm-1. In addition, we suggest that in LH2 of Rb. sphaeroides the angles made by the Qy transitions of the B850 BChls with respect to the plane of the ring are slightly different from those calculated from the crystal structure of the Rhodopseudomonas acidophila LH2 complex.